anno_start anno_end anno_text entity_type sentence section 24 34 Xyloglucan chemical Molecular Dissection of Xyloglucan Recognition in a Prominent Human Gut Symbiont TITLE 62 67 Human species Molecular Dissection of Xyloglucan Recognition in a Prominent Human Gut Symbiont TITLE 0 31 Polysaccharide utilization loci gene Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. ABSTRACT 33 36 PUL gene Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. ABSTRACT 69 74 human species Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. ABSTRACT 79 92 Bacteroidetes taxonomy_domain Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. ABSTRACT 161 174 carbohydrates chemical Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. ABSTRACT 241 244 PUL gene Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. ABSTRACT 339 344 human species Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. ABSTRACT 345 354 bacterial taxonomy_domain Polysaccharide utilization loci (PUL) within the genomes of resident human gut Bacteroidetes are central to the metabolism of the otherwise indigestible complex carbohydrates known as “dietary fiber.” However, functional characterization of PUL lags significantly behind sequencing efforts, which limits physiological understanding of the human-bacterial symbiosis. ABSTRACT 38 60 complex polysaccharide chemical In particular, the molecular basis of complex polysaccharide recognition, an essential prerequisite to hydrolysis by cell surface glycosidases and subsequent metabolism, is generally poorly understood. ABSTRACT 130 142 glycosidases protein_type In particular, the molecular basis of complex polysaccharide recognition, an essential prerequisite to hydrolysis by cell surface glycosidases and subsequent metabolism, is generally poorly understood. ABSTRACT 21 82 biochemical, structural, and reverse genetic characterization experimental_method Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. ABSTRACT 97 133 cell surface glycan-binding proteins protein_type Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. ABSTRACT 135 140 SGBPs protein_type Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. ABSTRACT 155 183 xyloglucan utilization locus gene Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. ABSTRACT 185 190 XyGUL gene Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. ABSTRACT 197 215 Bacteroides ovatus species Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. ABSTRACT 266 275 vegetable taxonomy_domain Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. ABSTRACT 276 290 polysaccharide chemical Here, we present the biochemical, structural, and reverse genetic characterization of two unique cell surface glycan-binding proteins (SGBPs) encoded by a xyloglucan utilization locus (XyGUL) from Bacteroides ovatus, which are integral to growth on this key dietary vegetable polysaccharide. ABSTRACT 0 20 Biochemical analysis experimental_method Biochemical analysis reveals that these outer membrane-anchored proteins are in fact exquisitely specific for the highly branched xyloglucan (XyG) polysaccharide. ABSTRACT 40 72 outer membrane-anchored proteins protein_type Biochemical analysis reveals that these outer membrane-anchored proteins are in fact exquisitely specific for the highly branched xyloglucan (XyG) polysaccharide. ABSTRACT 130 140 xyloglucan chemical Biochemical analysis reveals that these outer membrane-anchored proteins are in fact exquisitely specific for the highly branched xyloglucan (XyG) polysaccharide. ABSTRACT 142 145 XyG chemical Biochemical analysis reveals that these outer membrane-anchored proteins are in fact exquisitely specific for the highly branched xyloglucan (XyG) polysaccharide. ABSTRACT 147 161 polysaccharide chemical Biochemical analysis reveals that these outer membrane-anchored proteins are in fact exquisitely specific for the highly branched xyloglucan (XyG) polysaccharide. ABSTRACT 4 21 crystal structure evidence The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. ABSTRACT 25 31 SGBP-A protein The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. ABSTRACT 35 39 SusD protein The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. ABSTRACT 56 61 bound protein_state The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. ABSTRACT 62 65 XyG chemical The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. ABSTRACT 66 85 tetradecasaccharide chemical The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. ABSTRACT 106 135 carbohydrate-binding platform site The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. ABSTRACT 180 188 β-glucan chemical The crystal structure of SGBP-A, a SusD homolog, with a bound XyG tetradecasaccharide reveals an extended carbohydrate-binding platform that primarily relies on recognition of the β-glucan backbone. ABSTRACT 12 25 tetra-modular structure_element The unique, tetra-modular structure of SGBP-B is comprised of tandem Ig-like folds, with XyG binding mediated at the distal C-terminal domain. ABSTRACT 26 35 structure evidence The unique, tetra-modular structure of SGBP-B is comprised of tandem Ig-like folds, with XyG binding mediated at the distal C-terminal domain. ABSTRACT 39 45 SGBP-B protein The unique, tetra-modular structure of SGBP-B is comprised of tandem Ig-like folds, with XyG binding mediated at the distal C-terminal domain. ABSTRACT 62 82 tandem Ig-like folds structure_element The unique, tetra-modular structure of SGBP-B is comprised of tandem Ig-like folds, with XyG binding mediated at the distal C-terminal domain. ABSTRACT 89 92 XyG chemical The unique, tetra-modular structure of SGBP-B is comprised of tandem Ig-like folds, with XyG binding mediated at the distal C-terminal domain. ABSTRACT 124 141 C-terminal domain structure_element The unique, tetra-modular structure of SGBP-B is comprised of tandem Ig-like folds, with XyG binding mediated at the distal C-terminal domain. ABSTRACT 27 37 affinities evidence Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 42 45 XyG chemical Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 47 71 reverse-genetic analysis experimental_method Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 85 91 SGBP-B protein Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 146 162 oligosaccharides chemical Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 188 194 SGBP-A protein Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 221 233 carbohydrate chemical Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 264 267 XyG chemical Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 307 313 SGBP-A protein Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 318 324 SGBP-B protein Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 366 378 carbohydrate chemical Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 390 399 B. ovatus species Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 429 438 vegetable taxonomy_domain Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 439 450 xyloglucans chemical Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 471 484 Bacteroidetes taxonomy_domain Despite displaying similar affinities for XyG, reverse-genetic analysis reveals that SGBP-B is only required for the efficient capture of smaller oligosaccharides, whereas the presence of SGBP-A is more critical than its carbohydrate-binding ability for growth on XyG. Together, these data demonstrate that SGBP-A and SGBP-B play complementary, specialized roles in carbohydrate capture by B. ovatus and elaborate a model of how vegetable xyloglucans are accessed by the Bacteroidetes. ABSTRACT 4 17 Bacteroidetes taxonomy_domain The Bacteroidetes are dominant bacteria in the human gut that are responsible for the digestion of the complex polysaccharides that constitute “dietary fiber.” Although this symbiotic relationship has been appreciated for decades, little is currently known about how Bacteroidetes seek out and bind plant cell wall polysaccharides as a necessary first step in their metabolism. ABSTRACT 31 39 bacteria taxonomy_domain The Bacteroidetes are dominant bacteria in the human gut that are responsible for the digestion of the complex polysaccharides that constitute “dietary fiber.” Although this symbiotic relationship has been appreciated for decades, little is currently known about how Bacteroidetes seek out and bind plant cell wall polysaccharides as a necessary first step in their metabolism. ABSTRACT 47 52 human species The Bacteroidetes are dominant bacteria in the human gut that are responsible for the digestion of the complex polysaccharides that constitute “dietary fiber.” Although this symbiotic relationship has been appreciated for decades, little is currently known about how Bacteroidetes seek out and bind plant cell wall polysaccharides as a necessary first step in their metabolism. ABSTRACT 103 126 complex polysaccharides chemical The Bacteroidetes are dominant bacteria in the human gut that are responsible for the digestion of the complex polysaccharides that constitute “dietary fiber.” Although this symbiotic relationship has been appreciated for decades, little is currently known about how Bacteroidetes seek out and bind plant cell wall polysaccharides as a necessary first step in their metabolism. ABSTRACT 267 280 Bacteroidetes taxonomy_domain The Bacteroidetes are dominant bacteria in the human gut that are responsible for the digestion of the complex polysaccharides that constitute “dietary fiber.” Although this symbiotic relationship has been appreciated for decades, little is currently known about how Bacteroidetes seek out and bind plant cell wall polysaccharides as a necessary first step in their metabolism. ABSTRACT 299 304 plant taxonomy_domain The Bacteroidetes are dominant bacteria in the human gut that are responsible for the digestion of the complex polysaccharides that constitute “dietary fiber.” Although this symbiotic relationship has been appreciated for decades, little is currently known about how Bacteroidetes seek out and bind plant cell wall polysaccharides as a necessary first step in their metabolism. ABSTRACT 315 330 polysaccharides chemical The Bacteroidetes are dominant bacteria in the human gut that are responsible for the digestion of the complex polysaccharides that constitute “dietary fiber.” Although this symbiotic relationship has been appreciated for decades, little is currently known about how Bacteroidetes seek out and bind plant cell wall polysaccharides as a necessary first step in their metabolism. ABSTRACT 27 77 biochemical, crystallographic, and genetic insight experimental_method Here, we provide the first biochemical, crystallographic, and genetic insight into how two surface glycan-binding proteins from the complex Bacteroides ovatus xyloglucan utilization locus (XyGUL) enable recognition and uptake of this ubiquitous vegetable polysaccharide. ABSTRACT 91 122 surface glycan-binding proteins protein_type Here, we provide the first biochemical, crystallographic, and genetic insight into how two surface glycan-binding proteins from the complex Bacteroides ovatus xyloglucan utilization locus (XyGUL) enable recognition and uptake of this ubiquitous vegetable polysaccharide. ABSTRACT 140 158 Bacteroides ovatus species Here, we provide the first biochemical, crystallographic, and genetic insight into how two surface glycan-binding proteins from the complex Bacteroides ovatus xyloglucan utilization locus (XyGUL) enable recognition and uptake of this ubiquitous vegetable polysaccharide. ABSTRACT 159 187 xyloglucan utilization locus gene Here, we provide the first biochemical, crystallographic, and genetic insight into how two surface glycan-binding proteins from the complex Bacteroides ovatus xyloglucan utilization locus (XyGUL) enable recognition and uptake of this ubiquitous vegetable polysaccharide. ABSTRACT 189 194 XyGUL gene Here, we provide the first biochemical, crystallographic, and genetic insight into how two surface glycan-binding proteins from the complex Bacteroides ovatus xyloglucan utilization locus (XyGUL) enable recognition and uptake of this ubiquitous vegetable polysaccharide. ABSTRACT 245 254 vegetable taxonomy_domain Here, we provide the first biochemical, crystallographic, and genetic insight into how two surface glycan-binding proteins from the complex Bacteroides ovatus xyloglucan utilization locus (XyGUL) enable recognition and uptake of this ubiquitous vegetable polysaccharide. ABSTRACT 255 269 polysaccharide chemical Here, we provide the first biochemical, crystallographic, and genetic insight into how two surface glycan-binding proteins from the complex Bacteroides ovatus xyloglucan utilization locus (XyGUL) enable recognition and uptake of this ubiquitous vegetable polysaccharide. ABSTRACT 61 83 complex polysaccharide chemical Our combined analysis illuminates new fundamental aspects of complex polysaccharide recognition, cleavage, and import at the Bacteroidetes cell surface that may facilitate the development of prebiotics to target this phylum of gut bacteria. ABSTRACT 125 138 Bacteroidetes taxonomy_domain Our combined analysis illuminates new fundamental aspects of complex polysaccharide recognition, cleavage, and import at the Bacteroidetes cell surface that may facilitate the development of prebiotics to target this phylum of gut bacteria. ABSTRACT 231 239 bacteria taxonomy_domain Our combined analysis illuminates new fundamental aspects of complex polysaccharide recognition, cleavage, and import at the Bacteroidetes cell surface that may facilitate the development of prebiotics to target this phylum of gut bacteria. ABSTRACT 4 9 human species The human gut microbiota influences the course of human development and health, playing key roles in immune stimulation, intestinal cell proliferation, and metabolic balance. INTRO 14 24 microbiota taxonomy_domain The human gut microbiota influences the course of human development and health, playing key roles in immune stimulation, intestinal cell proliferation, and metabolic balance. INTRO 50 55 human species The human gut microbiota influences the course of human development and health, playing key roles in immune stimulation, intestinal cell proliferation, and metabolic balance. INTRO 5 14 microbial taxonomy_domain This microbial community is largely bacterial, with the Bacteroidetes, Firmicutes, and Actinobacteria comprising the dominant phyla. INTRO 36 45 bacterial taxonomy_domain This microbial community is largely bacterial, with the Bacteroidetes, Firmicutes, and Actinobacteria comprising the dominant phyla. INTRO 56 69 Bacteroidetes taxonomy_domain This microbial community is largely bacterial, with the Bacteroidetes, Firmicutes, and Actinobacteria comprising the dominant phyla. INTRO 71 81 Firmicutes taxonomy_domain This microbial community is largely bacterial, with the Bacteroidetes, Firmicutes, and Actinobacteria comprising the dominant phyla. INTRO 87 101 Actinobacteria taxonomy_domain This microbial community is largely bacterial, with the Bacteroidetes, Firmicutes, and Actinobacteria comprising the dominant phyla. INTRO 35 48 carbohydrates chemical The ability to acquire energy from carbohydrates of dietary or host origin is central to the adaptation of human gut bacterial species to their niche. INTRO 107 112 human species The ability to acquire energy from carbohydrates of dietary or host origin is central to the adaptation of human gut bacterial species to their niche. INTRO 117 126 bacterial taxonomy_domain The ability to acquire energy from carbohydrates of dietary or host origin is central to the adaptation of human gut bacterial species to their niche. INTRO 106 116 microbiota taxonomy_domain More importantly, this makes diet a tractable way to manipulate the abundance and metabolic output of the microbiota toward improved human health. INTRO 133 138 human species More importantly, this makes diet a tractable way to manipulate the abundance and metabolic output of the microbiota toward improved human health. INTRO 68 88 complex carbohydrate chemical However, there is a paucity of data regarding how the vast array of complex carbohydrate structures are selectively recognized and imported by members of the microbiota, a critical process that enables these organisms to thrive in the competitive gut environment. INTRO 158 168 microbiota taxonomy_domain However, there is a paucity of data regarding how the vast array of complex carbohydrate structures are selectively recognized and imported by members of the microbiota, a critical process that enables these organisms to thrive in the competitive gut environment. INTRO 4 9 human species The human gut bacteria Bacteroidetes share a profound capacity for dietary glycan degradation, with many species containing >250 predicted carbohydrate-active enzymes (CAZymes), compared to 50 to 100 within many Firmicutes and only 17 in the human genome devoted toward carbohydrate utilization. INTRO 14 22 bacteria taxonomy_domain The human gut bacteria Bacteroidetes share a profound capacity for dietary glycan degradation, with many species containing >250 predicted carbohydrate-active enzymes (CAZymes), compared to 50 to 100 within many Firmicutes and only 17 in the human genome devoted toward carbohydrate utilization. INTRO 23 36 Bacteroidetes taxonomy_domain The human gut bacteria Bacteroidetes share a profound capacity for dietary glycan degradation, with many species containing >250 predicted carbohydrate-active enzymes (CAZymes), compared to 50 to 100 within many Firmicutes and only 17 in the human genome devoted toward carbohydrate utilization. INTRO 75 81 glycan chemical The human gut bacteria Bacteroidetes share a profound capacity for dietary glycan degradation, with many species containing >250 predicted carbohydrate-active enzymes (CAZymes), compared to 50 to 100 within many Firmicutes and only 17 in the human genome devoted toward carbohydrate utilization. INTRO 212 222 Firmicutes taxonomy_domain The human gut bacteria Bacteroidetes share a profound capacity for dietary glycan degradation, with many species containing >250 predicted carbohydrate-active enzymes (CAZymes), compared to 50 to 100 within many Firmicutes and only 17 in the human genome devoted toward carbohydrate utilization. INTRO 242 247 human species The human gut bacteria Bacteroidetes share a profound capacity for dietary glycan degradation, with many species containing >250 predicted carbohydrate-active enzymes (CAZymes), compared to 50 to 100 within many Firmicutes and only 17 in the human genome devoted toward carbohydrate utilization. INTRO 28 41 Bacteroidetes taxonomy_domain A remarkable feature of the Bacteroidetes is the packaging of genes for carbohydrate catabolism into discrete polysaccharide utilization loci (PUL), which are transcriptionally regulated by specific substrate signatures. INTRO 110 141 polysaccharide utilization loci gene A remarkable feature of the Bacteroidetes is the packaging of genes for carbohydrate catabolism into discrete polysaccharide utilization loci (PUL), which are transcriptionally regulated by specific substrate signatures. INTRO 143 146 PUL gene A remarkable feature of the Bacteroidetes is the packaging of genes for carbohydrate catabolism into discrete polysaccharide utilization loci (PUL), which are transcriptionally regulated by specific substrate signatures. INTRO 15 18 PUL gene The archetypal PUL-encoded system is the starch utilization system (Sus) (Fig. 1B) of Bacteroides thetaiotaomicron. INTRO 41 66 starch utilization system complex_assembly The archetypal PUL-encoded system is the starch utilization system (Sus) (Fig. 1B) of Bacteroides thetaiotaomicron. INTRO 68 71 Sus complex_assembly The archetypal PUL-encoded system is the starch utilization system (Sus) (Fig. 1B) of Bacteroides thetaiotaomicron. INTRO 86 114 Bacteroides thetaiotaomicron species The archetypal PUL-encoded system is the starch utilization system (Sus) (Fig. 1B) of Bacteroides thetaiotaomicron. INTRO 4 7 Sus complex_assembly The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 19 33 lipid-anchored protein_state The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 50 62 endo-amylase protein_type The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 64 68 SusG protein The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 72 98 TonB-dependent transporter protein_type The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 100 104 TBDT protein_type The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 107 111 SusC protein The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 127 143 oligosaccharides chemical The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 175 197 starch-binding protein protein_type The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 199 203 SusD protein The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 220 253 carbohydrate-binding lipoproteins protein_type The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 255 259 SusE protein The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 264 268 SusF protein The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 290 306 exo-glucosidases protein_type The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 308 312 SusA protein The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 317 321 SusB protein The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 338 345 glucose chemical The Sus includes a lipid-anchored, outer membrane endo-amylase, SusG; a TonB-dependent transporter (TBDT), SusC, which imports oligosaccharides with the help of an associated starch-binding protein, SusD; two additional carbohydrate-binding lipoproteins, SusE and SusF; and two periplasmic exo-glucosidases, SusA and SusB, which generate glucose for transport into the cytoplasm. INTRO 18 21 PUL gene The importance of PUL as a successful evolutionary strategy is underscored by the observation that Bacteroidetes such as B. thetaiotaomicron and Bacteroides ovatus devote ~18% of their genomes to these systems. INTRO 99 112 Bacteroidetes taxonomy_domain The importance of PUL as a successful evolutionary strategy is underscored by the observation that Bacteroidetes such as B. thetaiotaomicron and Bacteroides ovatus devote ~18% of their genomes to these systems. INTRO 121 140 B. thetaiotaomicron species The importance of PUL as a successful evolutionary strategy is underscored by the observation that Bacteroidetes such as B. thetaiotaomicron and Bacteroides ovatus devote ~18% of their genomes to these systems. INTRO 145 163 Bacteroides ovatus species The importance of PUL as a successful evolutionary strategy is underscored by the observation that Bacteroidetes such as B. thetaiotaomicron and Bacteroides ovatus devote ~18% of their genomes to these systems. INTRO 88 91 PUL gene Moving beyond seminal genomic and transcriptomic analyses, the current state-of-the-art PUL characterization involves combined reverse-genetic, biochemical, and structural studies to illuminate the molecular details of PUL function. INTRO 127 179 reverse-genetic, biochemical, and structural studies experimental_method Moving beyond seminal genomic and transcriptomic analyses, the current state-of-the-art PUL characterization involves combined reverse-genetic, biochemical, and structural studies to illuminate the molecular details of PUL function. INTRO 219 222 PUL gene Moving beyond seminal genomic and transcriptomic analyses, the current state-of-the-art PUL characterization involves combined reverse-genetic, biochemical, and structural studies to illuminate the molecular details of PUL function. INTRO 0 10 Xyloglucan chemical Xyloglucan and the Bacteroides ovatus xyloglucan utilization locus (XyGUL). (A) Representative structures of common xyloglucans using the Consortium for Functional Glycomics Symbol Nomenclature (http://www.functionalglycomics.org/static/consortium/Nomenclature.shtml). FIG 19 37 Bacteroides ovatus species Xyloglucan and the Bacteroides ovatus xyloglucan utilization locus (XyGUL). (A) Representative structures of common xyloglucans using the Consortium for Functional Glycomics Symbol Nomenclature (http://www.functionalglycomics.org/static/consortium/Nomenclature.shtml). FIG 38 66 xyloglucan utilization locus gene Xyloglucan and the Bacteroides ovatus xyloglucan utilization locus (XyGUL). (A) Representative structures of common xyloglucans using the Consortium for Functional Glycomics Symbol Nomenclature (http://www.functionalglycomics.org/static/consortium/Nomenclature.shtml). FIG 68 73 XyGUL gene Xyloglucan and the Bacteroides ovatus xyloglucan utilization locus (XyGUL). (A) Representative structures of common xyloglucans using the Consortium for Functional Glycomics Symbol Nomenclature (http://www.functionalglycomics.org/static/consortium/Nomenclature.shtml). FIG 95 105 structures evidence Xyloglucan and the Bacteroides ovatus xyloglucan utilization locus (XyGUL). (A) Representative structures of common xyloglucans using the Consortium for Functional Glycomics Symbol Nomenclature (http://www.functionalglycomics.org/static/consortium/Nomenclature.shtml). FIG 116 127 xyloglucans chemical Xyloglucan and the Bacteroides ovatus xyloglucan utilization locus (XyGUL). (A) Representative structures of common xyloglucans using the Consortium for Functional Glycomics Symbol Nomenclature (http://www.functionalglycomics.org/static/consortium/Nomenclature.shtml). FIG 19 26 BoXyGUL gene Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 27 39 glycosidases protein_type Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 41 44 GHs protein_type Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 64 75 solanaceous taxonomy_domain Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 76 86 xyloglucan chemical Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 92 97 BtSus gene Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 102 109 BoXyGUL gene Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 131 138 BoXyGUL gene Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 230 241 xyloglucans chemical Cleavage sites for BoXyGUL glycosidases (GHs) are indicated for solanaceous xyloglucan. (B) BtSus and BoXyGUL. (C) Localization of BoXyGUL-encoded proteins in cellular membranes and concerted modes of action in the degradation of xyloglucans to monosaccharides. FIG 16 22 SGBP-A protein The location of SGBP-A/B is presented in this work; the location of GH5 has been empirically determined, and the enzymes have been placed based upon their predicted cellular location. FIG 23 24 B protein The location of SGBP-A/B is presented in this work; the location of GH5 has been empirically determined, and the enzymes have been placed based upon their predicted cellular location. FIG 68 71 GH5 protein The location of SGBP-A/B is presented in this work; the location of GH5 has been empirically determined, and the enzymes have been placed based upon their predicted cellular location. FIG 66 69 PUL gene We recently reported the detailed molecular characterization of a PUL that confers the ability of the human gut commensal B. ovatus ATCC 8483 to grow on a prominent family of plant cell wall glycans, the xyloglucans (XyG). INTRO 102 107 human species We recently reported the detailed molecular characterization of a PUL that confers the ability of the human gut commensal B. ovatus ATCC 8483 to grow on a prominent family of plant cell wall glycans, the xyloglucans (XyG). INTRO 122 141 B. ovatus ATCC 8483 species We recently reported the detailed molecular characterization of a PUL that confers the ability of the human gut commensal B. ovatus ATCC 8483 to grow on a prominent family of plant cell wall glycans, the xyloglucans (XyG). INTRO 175 180 plant taxonomy_domain We recently reported the detailed molecular characterization of a PUL that confers the ability of the human gut commensal B. ovatus ATCC 8483 to grow on a prominent family of plant cell wall glycans, the xyloglucans (XyG). INTRO 191 198 glycans chemical We recently reported the detailed molecular characterization of a PUL that confers the ability of the human gut commensal B. ovatus ATCC 8483 to grow on a prominent family of plant cell wall glycans, the xyloglucans (XyG). INTRO 204 215 xyloglucans chemical We recently reported the detailed molecular characterization of a PUL that confers the ability of the human gut commensal B. ovatus ATCC 8483 to grow on a prominent family of plant cell wall glycans, the xyloglucans (XyG). INTRO 217 220 XyG chemical We recently reported the detailed molecular characterization of a PUL that confers the ability of the human gut commensal B. ovatus ATCC 8483 to grow on a prominent family of plant cell wall glycans, the xyloglucans (XyG). INTRO 0 3 XyG chemical XyG variants (Fig. 1A) constitute up to 25% of the dry weight of common vegetables. INTRO 72 82 vegetables taxonomy_domain XyG variants (Fig. 1A) constitute up to 25% of the dry weight of common vegetables. INTRO 17 26 Sus locus gene Analogous to the Sus locus, the xyloglucan utilization locus (XyGUL) encodes a cohort of carbohydrate-binding, -hydrolyzing, and -importing proteins (Fig. 1B and C). INTRO 32 60 xyloglucan utilization locus gene Analogous to the Sus locus, the xyloglucan utilization locus (XyGUL) encodes a cohort of carbohydrate-binding, -hydrolyzing, and -importing proteins (Fig. 1B and C). INTRO 62 67 XyGUL gene Analogous to the Sus locus, the xyloglucan utilization locus (XyGUL) encodes a cohort of carbohydrate-binding, -hydrolyzing, and -importing proteins (Fig. 1B and C). INTRO 89 148 carbohydrate-binding, -hydrolyzing, and -importing proteins protein_type Analogous to the Sus locus, the xyloglucan utilization locus (XyGUL) encodes a cohort of carbohydrate-binding, -hydrolyzing, and -importing proteins (Fig. 1B and C). INTRO 14 34 glycoside hydrolases protein_type The number of glycoside hydrolases (GHs) encoded by the XyGUL is, however, more expansive than that by the Sus locus (Fig. 1B), which reflects the greater complexity of glycosidic linkages found in XyG vis-à-vis starch. INTRO 36 39 GHs protein_type The number of glycoside hydrolases (GHs) encoded by the XyGUL is, however, more expansive than that by the Sus locus (Fig. 1B), which reflects the greater complexity of glycosidic linkages found in XyG vis-à-vis starch. INTRO 56 61 XyGUL gene The number of glycoside hydrolases (GHs) encoded by the XyGUL is, however, more expansive than that by the Sus locus (Fig. 1B), which reflects the greater complexity of glycosidic linkages found in XyG vis-à-vis starch. INTRO 107 116 Sus locus gene The number of glycoside hydrolases (GHs) encoded by the XyGUL is, however, more expansive than that by the Sus locus (Fig. 1B), which reflects the greater complexity of glycosidic linkages found in XyG vis-à-vis starch. INTRO 198 201 XyG chemical The number of glycoside hydrolases (GHs) encoded by the XyGUL is, however, more expansive than that by the Sus locus (Fig. 1B), which reflects the greater complexity of glycosidic linkages found in XyG vis-à-vis starch. INTRO 212 218 starch chemical The number of glycoside hydrolases (GHs) encoded by the XyGUL is, however, more expansive than that by the Sus locus (Fig. 1B), which reflects the greater complexity of glycosidic linkages found in XyG vis-à-vis starch. INTRO 95 98 GHs protein_type Whereas our previous study focused on the characterization of the linkage specificity of these GHs, a key outstanding question regarding this locus is how XyG recognition is mediated at the cell surface. INTRO 155 158 XyG chemical Whereas our previous study focused on the characterization of the linkage specificity of these GHs, a key outstanding question regarding this locus is how XyG recognition is mediated at the cell surface. INTRO 18 43 starch utilization system complex_assembly In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 47 66 B. thetaiotaomicron species In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 133 153 starch-binding sites site In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 177 208 surface glycan-binding proteins protein_type In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 210 215 SGBPs protein_type In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 233 240 amylase protein_type In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 241 245 SusG protein In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 258 262 SusD protein In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 275 279 SusE protein In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 298 302 SusF protein In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 370 374 SusD protein In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 402 408 starch chemical In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 436 440 SusE protein In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 442 446 SusF protein In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 452 456 SusG protein In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 457 470 binding sites site In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 508 522 polysaccharide chemical In the archetypal starch utilization system of B. thetaiotaomicron, starch binding to the cell surface is mediated at eight distinct starch-binding sites distributed among four surface glycan-binding proteins (SGBPs): two within the amylase SusG, one within SusD, two within SusE, and three within SusF. The functional redundancy of many of these sites is high: whereas SusD is essential for growth on starch, combined mutations of the SusE, SusF, and SusG binding sites are required to impair growth on the polysaccharide. INTRO 0 13 Bacteroidetes taxonomy_domain Bacteroidetes PUL ubiquitously encode homologs of SusC and SusD, as well as proteins whose genes are immediately downstream of susD, akin to susE/F, and these are typically annotated as “putative lipoproteins”. INTRO 14 17 PUL gene Bacteroidetes PUL ubiquitously encode homologs of SusC and SusD, as well as proteins whose genes are immediately downstream of susD, akin to susE/F, and these are typically annotated as “putative lipoproteins”. INTRO 50 54 SusC protein Bacteroidetes PUL ubiquitously encode homologs of SusC and SusD, as well as proteins whose genes are immediately downstream of susD, akin to susE/F, and these are typically annotated as “putative lipoproteins”. INTRO 59 63 SusD protein Bacteroidetes PUL ubiquitously encode homologs of SusC and SusD, as well as proteins whose genes are immediately downstream of susD, akin to susE/F, and these are typically annotated as “putative lipoproteins”. INTRO 127 131 susD gene Bacteroidetes PUL ubiquitously encode homologs of SusC and SusD, as well as proteins whose genes are immediately downstream of susD, akin to susE/F, and these are typically annotated as “putative lipoproteins”. INTRO 141 147 susE/F gene Bacteroidetes PUL ubiquitously encode homologs of SusC and SusD, as well as proteins whose genes are immediately downstream of susD, akin to susE/F, and these are typically annotated as “putative lipoproteins”. INTRO 187 195 putative protein_state Bacteroidetes PUL ubiquitously encode homologs of SusC and SusD, as well as proteins whose genes are immediately downstream of susD, akin to susE/F, and these are typically annotated as “putative lipoproteins”. INTRO 196 208 lipoproteins protein_type Bacteroidetes PUL ubiquitously encode homologs of SusC and SusD, as well as proteins whose genes are immediately downstream of susD, akin to susE/F, and these are typically annotated as “putative lipoproteins”. INTRO 63 69 susE/F gene The genes coding for these proteins, sometimes referred to as “susE/F positioned,” display products with a wide variation in amino acid sequence and which have little or no homology to other PUL-encoded proteins or known carbohydrate-binding proteins. INTRO 191 194 PUL gene The genes coding for these proteins, sometimes referred to as “susE/F positioned,” display products with a wide variation in amino acid sequence and which have little or no homology to other PUL-encoded proteins or known carbohydrate-binding proteins. INTRO 221 250 carbohydrate-binding proteins protein_type The genes coding for these proteins, sometimes referred to as “susE/F positioned,” display products with a wide variation in amino acid sequence and which have little or no homology to other PUL-encoded proteins or known carbohydrate-binding proteins. INTRO 7 10 Sus complex_assembly As the Sus SGBPs remain the only structurally characterized cohort to date, we therefore wondered whether such glycan binding and function are extended to other PUL that target more complex and heterogeneous polysaccharides, such as XyG. INTRO 11 16 SGBPs protein_type As the Sus SGBPs remain the only structurally characterized cohort to date, we therefore wondered whether such glycan binding and function are extended to other PUL that target more complex and heterogeneous polysaccharides, such as XyG. INTRO 111 117 glycan chemical As the Sus SGBPs remain the only structurally characterized cohort to date, we therefore wondered whether such glycan binding and function are extended to other PUL that target more complex and heterogeneous polysaccharides, such as XyG. INTRO 161 164 PUL gene As the Sus SGBPs remain the only structurally characterized cohort to date, we therefore wondered whether such glycan binding and function are extended to other PUL that target more complex and heterogeneous polysaccharides, such as XyG. INTRO 208 223 polysaccharides chemical As the Sus SGBPs remain the only structurally characterized cohort to date, we therefore wondered whether such glycan binding and function are extended to other PUL that target more complex and heterogeneous polysaccharides, such as XyG. INTRO 233 236 XyG chemical As the Sus SGBPs remain the only structurally characterized cohort to date, we therefore wondered whether such glycan binding and function are extended to other PUL that target more complex and heterogeneous polysaccharides, such as XyG. INTRO 30 72 functional and structural characterization experimental_method We describe here the detailed functional and structural characterization of the noncatalytic SGBPs encoded by Bacova_02651 and Bacova_02650 of the XyGUL, here referred to as SGBP-A and SGBP-B, to elucidate their molecular roles in carbohydrate acquisition in vivo. INTRO 80 92 noncatalytic protein_state We describe here the detailed functional and structural characterization of the noncatalytic SGBPs encoded by Bacova_02651 and Bacova_02650 of the XyGUL, here referred to as SGBP-A and SGBP-B, to elucidate their molecular roles in carbohydrate acquisition in vivo. INTRO 93 98 SGBPs protein_type We describe here the detailed functional and structural characterization of the noncatalytic SGBPs encoded by Bacova_02651 and Bacova_02650 of the XyGUL, here referred to as SGBP-A and SGBP-B, to elucidate their molecular roles in carbohydrate acquisition in vivo. INTRO 110 122 Bacova_02651 gene We describe here the detailed functional and structural characterization of the noncatalytic SGBPs encoded by Bacova_02651 and Bacova_02650 of the XyGUL, here referred to as SGBP-A and SGBP-B, to elucidate their molecular roles in carbohydrate acquisition in vivo. INTRO 127 139 Bacova_02650 gene We describe here the detailed functional and structural characterization of the noncatalytic SGBPs encoded by Bacova_02651 and Bacova_02650 of the XyGUL, here referred to as SGBP-A and SGBP-B, to elucidate their molecular roles in carbohydrate acquisition in vivo. INTRO 147 152 XyGUL gene We describe here the detailed functional and structural characterization of the noncatalytic SGBPs encoded by Bacova_02651 and Bacova_02650 of the XyGUL, here referred to as SGBP-A and SGBP-B, to elucidate their molecular roles in carbohydrate acquisition in vivo. INTRO 174 180 SGBP-A protein We describe here the detailed functional and structural characterization of the noncatalytic SGBPs encoded by Bacova_02651 and Bacova_02650 of the XyGUL, here referred to as SGBP-A and SGBP-B, to elucidate their molecular roles in carbohydrate acquisition in vivo. INTRO 185 191 SGBP-B protein We describe here the detailed functional and structural characterization of the noncatalytic SGBPs encoded by Bacova_02651 and Bacova_02650 of the XyGUL, here referred to as SGBP-A and SGBP-B, to elucidate their molecular roles in carbohydrate acquisition in vivo. INTRO 9 64 biochemical, structural, and reverse-genetic approaches experimental_method Combined biochemical, structural, and reverse-genetic approaches clearly illuminate the distinct, yet complementary, functions that these two proteins play in XyG recognition as it impacts the physiology of B. ovatus. INTRO 159 162 XyG chemical Combined biochemical, structural, and reverse-genetic approaches clearly illuminate the distinct, yet complementary, functions that these two proteins play in XyG recognition as it impacts the physiology of B. ovatus. INTRO 207 216 B. ovatus species Combined biochemical, structural, and reverse-genetic approaches clearly illuminate the distinct, yet complementary, functions that these two proteins play in XyG recognition as it impacts the physiology of B. ovatus. INTRO 60 66 glycan chemical These data extend our current understanding of the Sus-like glycan uptake paradigm within the Bacteroidetes and reveals how the complex dietary polysaccharide xyloglucan is recognized at the cell surface. INTRO 94 107 Bacteroidetes taxonomy_domain These data extend our current understanding of the Sus-like glycan uptake paradigm within the Bacteroidetes and reveals how the complex dietary polysaccharide xyloglucan is recognized at the cell surface. INTRO 144 158 polysaccharide chemical These data extend our current understanding of the Sus-like glycan uptake paradigm within the Bacteroidetes and reveals how the complex dietary polysaccharide xyloglucan is recognized at the cell surface. INTRO 159 169 xyloglucan chemical These data extend our current understanding of the Sus-like glycan uptake paradigm within the Bacteroidetes and reveals how the complex dietary polysaccharide xyloglucan is recognized at the cell surface. INTRO 0 6 SGBP-A protein SGBP-A and SGBP-B are cell-surface-localized, xyloglucan-specific binding proteins. RESULTS 11 17 SGBP-B protein SGBP-A and SGBP-B are cell-surface-localized, xyloglucan-specific binding proteins. RESULTS 22 82 cell-surface-localized, xyloglucan-specific binding proteins protein_type SGBP-A and SGBP-B are cell-surface-localized, xyloglucan-specific binding proteins. RESULTS 0 6 SGBP-A protein SGBP-A, encoded by the XyGUL locus tag Bacova_02651 (Fig. 1B), shares 26% amino acid sequence identity (40% similarity) with its homolog, B. thetaiotaomicron SusD, and similar homology with the SusD-like proteins encoded within syntenic XyGUL identified in our earlier work. RESULTS 23 28 XyGUL gene SGBP-A, encoded by the XyGUL locus tag Bacova_02651 (Fig. 1B), shares 26% amino acid sequence identity (40% similarity) with its homolog, B. thetaiotaomicron SusD, and similar homology with the SusD-like proteins encoded within syntenic XyGUL identified in our earlier work. RESULTS 39 51 Bacova_02651 gene SGBP-A, encoded by the XyGUL locus tag Bacova_02651 (Fig. 1B), shares 26% amino acid sequence identity (40% similarity) with its homolog, B. thetaiotaomicron SusD, and similar homology with the SusD-like proteins encoded within syntenic XyGUL identified in our earlier work. RESULTS 138 157 B. thetaiotaomicron species SGBP-A, encoded by the XyGUL locus tag Bacova_02651 (Fig. 1B), shares 26% amino acid sequence identity (40% similarity) with its homolog, B. thetaiotaomicron SusD, and similar homology with the SusD-like proteins encoded within syntenic XyGUL identified in our earlier work. RESULTS 158 162 SusD protein SGBP-A, encoded by the XyGUL locus tag Bacova_02651 (Fig. 1B), shares 26% amino acid sequence identity (40% similarity) with its homolog, B. thetaiotaomicron SusD, and similar homology with the SusD-like proteins encoded within syntenic XyGUL identified in our earlier work. RESULTS 194 212 SusD-like proteins protein_type SGBP-A, encoded by the XyGUL locus tag Bacova_02651 (Fig. 1B), shares 26% amino acid sequence identity (40% similarity) with its homolog, B. thetaiotaomicron SusD, and similar homology with the SusD-like proteins encoded within syntenic XyGUL identified in our earlier work. RESULTS 237 242 XyGUL gene SGBP-A, encoded by the XyGUL locus tag Bacova_02651 (Fig. 1B), shares 26% amino acid sequence identity (40% similarity) with its homolog, B. thetaiotaomicron SusD, and similar homology with the SusD-like proteins encoded within syntenic XyGUL identified in our earlier work. RESULTS 13 19 SGBP-B protein In contrast, SGBP-B, encoded by locus tag Bacova_02650, displays little sequence similarity to the products of similarly positioned genes in syntenic XyGUL nor to any other gene product among the diversity of Bacteroidetes PUL. RESULTS 42 54 Bacova_02650 gene In contrast, SGBP-B, encoded by locus tag Bacova_02650, displays little sequence similarity to the products of similarly positioned genes in syntenic XyGUL nor to any other gene product among the diversity of Bacteroidetes PUL. RESULTS 150 155 XyGUL gene In contrast, SGBP-B, encoded by locus tag Bacova_02650, displays little sequence similarity to the products of similarly positioned genes in syntenic XyGUL nor to any other gene product among the diversity of Bacteroidetes PUL. RESULTS 209 222 Bacteroidetes taxonomy_domain In contrast, SGBP-B, encoded by locus tag Bacova_02650, displays little sequence similarity to the products of similarly positioned genes in syntenic XyGUL nor to any other gene product among the diversity of Bacteroidetes PUL. RESULTS 223 226 PUL gene In contrast, SGBP-B, encoded by locus tag Bacova_02650, displays little sequence similarity to the products of similarly positioned genes in syntenic XyGUL nor to any other gene product among the diversity of Bacteroidetes PUL. RESULTS 34 38 SusC protein Whereas sequence similarity among SusC/SusD homolog pairs often serves as a hallmark for PUL identification, the sequence similarities of downstream genes encoding SGBPs are generally too low to allow reliable bioinformatic classification of their products into protein families, let alone prediction of function. RESULTS 39 43 SusD protein Whereas sequence similarity among SusC/SusD homolog pairs often serves as a hallmark for PUL identification, the sequence similarities of downstream genes encoding SGBPs are generally too low to allow reliable bioinformatic classification of their products into protein families, let alone prediction of function. RESULTS 89 92 PUL gene Whereas sequence similarity among SusC/SusD homolog pairs often serves as a hallmark for PUL identification, the sequence similarities of downstream genes encoding SGBPs are generally too low to allow reliable bioinformatic classification of their products into protein families, let alone prediction of function. RESULTS 164 169 SGBPs protein_type Whereas sequence similarity among SusC/SusD homolog pairs often serves as a hallmark for PUL identification, the sequence similarities of downstream genes encoding SGBPs are generally too low to allow reliable bioinformatic classification of their products into protein families, let alone prediction of function. RESULTS 103 106 PUL gene Hence, there is a critical need for the elucidation of detailed structure-function relationships among PUL SGBPs, in light of the manifold glycan structures in nature. RESULTS 107 112 SGBPs protein_type Hence, there is a critical need for the elucidation of detailed structure-function relationships among PUL SGBPs, in light of the manifold glycan structures in nature. RESULTS 139 145 glycan chemical Hence, there is a critical need for the elucidation of detailed structure-function relationships among PUL SGBPs, in light of the manifold glycan structures in nature. RESULTS 0 18 Immunofluorescence experimental_method Immunofluorescence of formaldehyde-fixed, nonpermeabilized cells grown in minimal medium with XyG as the sole carbon source to induce XyGUL expression, reveals that both SGBP-A and SGBP-B are presented on the cell surface by N-terminal lipidation, as predicted by signal peptide analysis with SignalP (Fig. 2). RESULTS 94 97 XyG chemical Immunofluorescence of formaldehyde-fixed, nonpermeabilized cells grown in minimal medium with XyG as the sole carbon source to induce XyGUL expression, reveals that both SGBP-A and SGBP-B are presented on the cell surface by N-terminal lipidation, as predicted by signal peptide analysis with SignalP (Fig. 2). RESULTS 134 139 XyGUL gene Immunofluorescence of formaldehyde-fixed, nonpermeabilized cells grown in minimal medium with XyG as the sole carbon source to induce XyGUL expression, reveals that both SGBP-A and SGBP-B are presented on the cell surface by N-terminal lipidation, as predicted by signal peptide analysis with SignalP (Fig. 2). RESULTS 170 176 SGBP-A protein Immunofluorescence of formaldehyde-fixed, nonpermeabilized cells grown in minimal medium with XyG as the sole carbon source to induce XyGUL expression, reveals that both SGBP-A and SGBP-B are presented on the cell surface by N-terminal lipidation, as predicted by signal peptide analysis with SignalP (Fig. 2). RESULTS 181 187 SGBP-B protein Immunofluorescence of formaldehyde-fixed, nonpermeabilized cells grown in minimal medium with XyG as the sole carbon source to induce XyGUL expression, reveals that both SGBP-A and SGBP-B are presented on the cell surface by N-terminal lipidation, as predicted by signal peptide analysis with SignalP (Fig. 2). RESULTS 236 246 lipidation ptm Immunofluorescence of formaldehyde-fixed, nonpermeabilized cells grown in minimal medium with XyG as the sole carbon source to induce XyGUL expression, reveals that both SGBP-A and SGBP-B are presented on the cell surface by N-terminal lipidation, as predicted by signal peptide analysis with SignalP (Fig. 2). RESULTS 10 15 SGBPs protein_type Here, the SGBPs very likely work in concert with the cell-surface-localized endo-xyloglucanase B. ovatus GH5 (BoGH5) to recruit and cleave XyG for subsequent periplasmic import via the SusC-like TBDT of the XyGUL (Fig. 1B and C). RESULTS 53 94 cell-surface-localized endo-xyloglucanase protein_type Here, the SGBPs very likely work in concert with the cell-surface-localized endo-xyloglucanase B. ovatus GH5 (BoGH5) to recruit and cleave XyG for subsequent periplasmic import via the SusC-like TBDT of the XyGUL (Fig. 1B and C). RESULTS 95 104 B. ovatus species Here, the SGBPs very likely work in concert with the cell-surface-localized endo-xyloglucanase B. ovatus GH5 (BoGH5) to recruit and cleave XyG for subsequent periplasmic import via the SusC-like TBDT of the XyGUL (Fig. 1B and C). RESULTS 105 108 GH5 protein Here, the SGBPs very likely work in concert with the cell-surface-localized endo-xyloglucanase B. ovatus GH5 (BoGH5) to recruit and cleave XyG for subsequent periplasmic import via the SusC-like TBDT of the XyGUL (Fig. 1B and C). RESULTS 110 115 BoGH5 protein Here, the SGBPs very likely work in concert with the cell-surface-localized endo-xyloglucanase B. ovatus GH5 (BoGH5) to recruit and cleave XyG for subsequent periplasmic import via the SusC-like TBDT of the XyGUL (Fig. 1B and C). RESULTS 139 142 XyG chemical Here, the SGBPs very likely work in concert with the cell-surface-localized endo-xyloglucanase B. ovatus GH5 (BoGH5) to recruit and cleave XyG for subsequent periplasmic import via the SusC-like TBDT of the XyGUL (Fig. 1B and C). RESULTS 185 199 SusC-like TBDT protein_type Here, the SGBPs very likely work in concert with the cell-surface-localized endo-xyloglucanase B. ovatus GH5 (BoGH5) to recruit and cleave XyG for subsequent periplasmic import via the SusC-like TBDT of the XyGUL (Fig. 1B and C). RESULTS 207 212 XyGUL gene Here, the SGBPs very likely work in concert with the cell-surface-localized endo-xyloglucanase B. ovatus GH5 (BoGH5) to recruit and cleave XyG for subsequent periplasmic import via the SusC-like TBDT of the XyGUL (Fig. 1B and C). RESULTS 0 6 SGBP-A protein SGBP-A and SGBP-B visualized by immunofluorescence. FIG 11 17 SGBP-B protein SGBP-A and SGBP-B visualized by immunofluorescence. FIG 32 50 immunofluorescence experimental_method SGBP-A and SGBP-B visualized by immunofluorescence. FIG 33 42 B. ovatus species Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 83 86 XyG chemical Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 128 134 SGBP-A protein Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 138 144 SGBP-B protein Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 210 217 Overlay experimental_method Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 221 249 bright-field and FITC images evidence Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 253 262 B. ovatus species Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 299 306 Overlay experimental_method Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 310 338 bright-field and FITC images evidence Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 342 351 B. ovatus species Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 388 406 Bright-field image evidence Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 410 417 ΔSGBP-B mutant Formalin-fixed, nonpermeabilized B. ovatus cells were grown in minimal medium plus XyG, probed with custom rabbit antibodies to SGBP-A or SGBP-B, and then stained with Alexa Fluor 488 goat anti-rabbit IgG. (A) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-A. (B) Overlay of bright-field and FITC images of B. ovatus cells labeled with anti-SGBP-B. (C) Bright-field image of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 4 15 FITC images evidence (D) FITC images of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 19 26 ΔSGBP-B mutant (D) FITC images of ΔSGBP-B cells labeled with anti-SGBP-B antibodies. FIG 6 13 lacking protein_state Cells lacking SGBP-A (ΔSGBP-A) do not grow on XyG and therefore could not be tested in parallel. FIG 14 20 SGBP-A protein Cells lacking SGBP-A (ΔSGBP-A) do not grow on XyG and therefore could not be tested in parallel. FIG 22 29 ΔSGBP-A mutant Cells lacking SGBP-A (ΔSGBP-A) do not grow on XyG and therefore could not be tested in parallel. FIG 46 49 XyG chemical Cells lacking SGBP-A (ΔSGBP-A) do not grow on XyG and therefore could not be tested in parallel. FIG 71 91 glycoside hydrolases protein_type In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 99 104 XyGUL gene In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 130 143 affinity PAGE experimental_method In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 148 180 isothermal titration calorimetry experimental_method In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 182 185 ITC experimental_method In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 213 219 SGBP-A protein In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 224 230 SGBP-B protein In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 245 272 xyloglucan-binding proteins protein_type In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 274 291 affinity constant evidence In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 293 295 Ka evidence In our initial study focused on the functional characterization of the glycoside hydrolases of the XyGUL, we reported preliminary affinity PAGE and isothermal titration calorimetry (ITC) data indicating that both SGBP-A and SGBP-B are competent xyloglucan-binding proteins (affinity constant [Ka] values of 3.74 × 105 M−1 and 4.98 × 104 M−1, respectively [23]). RESULTS 11 24 affinity PAGE experimental_method Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 61 67 SGBP-A protein Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 143 165 hydroxyethyl cellulose chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 167 170 HEC chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 174 189 β(1 → 4)-glucan chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 216 250 mixed-linkage β(1→3)/β(1→4)-glucan chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 252 255 MLG chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 261 272 glucomannan chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 274 276 GM chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 284 292 glucosyl chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 297 305 mannosyl chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 360 374 polysaccharide chemical Additional affinity PAGE analysis (Fig. 3) demonstrates that SGBP-A also has moderate affinity for the artificial soluble cellulose derivative hydroxyethyl cellulose [HEC; a β(1 → 4)-glucan] and limited affinity for mixed-linkage β(1→3)/β(1→4)-glucan (MLG) and glucomannan (GM; mixed glucosyl and mannosyl backbone), which together indicate general binding to polysaccharide backbone residues and major contributions from side-chain recognition. RESULTS 13 19 SGBP-B protein In contrast, SGBP-B bound to HEC more weakly than SGBP-A and did not bind to MLG or GM. RESULTS 29 32 HEC chemical In contrast, SGBP-B bound to HEC more weakly than SGBP-A and did not bind to MLG or GM. RESULTS 50 56 SGBP-A protein In contrast, SGBP-B bound to HEC more weakly than SGBP-A and did not bind to MLG or GM. RESULTS 77 80 MLG chemical In contrast, SGBP-B bound to HEC more weakly than SGBP-A and did not bind to MLG or GM. RESULTS 84 86 GM chemical In contrast, SGBP-B bound to HEC more weakly than SGBP-A and did not bind to MLG or GM. RESULTS 8 12 SGBP protein_type Neither SGBP recognized galactomannan (GGM), starch, carboxymethylcellulose, or mucin (see Fig. S1 in the supplemental material). RESULTS 24 37 galactomannan chemical Neither SGBP recognized galactomannan (GGM), starch, carboxymethylcellulose, or mucin (see Fig. S1 in the supplemental material). RESULTS 39 42 GGM chemical Neither SGBP recognized galactomannan (GGM), starch, carboxymethylcellulose, or mucin (see Fig. S1 in the supplemental material). RESULTS 45 51 starch chemical Neither SGBP recognized galactomannan (GGM), starch, carboxymethylcellulose, or mucin (see Fig. S1 in the supplemental material). RESULTS 53 75 carboxymethylcellulose chemical Neither SGBP recognized galactomannan (GGM), starch, carboxymethylcellulose, or mucin (see Fig. S1 in the supplemental material). RESULTS 80 85 mucin chemical Neither SGBP recognized galactomannan (GGM), starch, carboxymethylcellulose, or mucin (see Fig. S1 in the supplemental material). RESULTS 60 66 SGBP-A protein Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 71 77 SGBP-B protein Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 82 85 XyG chemical Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 135 151 XyG-specific GHs protein_type Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 159 164 XyGUL gene Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 217 226 B. ovatus species Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 240 243 PUL gene Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 248 251 MLG chemical Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 253 255 GM chemical Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 261 264 GGM chemical Together, these results highlight the high specificities of SGBP-A and SGBP-B for XyG, which is concordant with their association with XyG-specific GHs in the XyGUL, as well as transcriptomic analysis indicating that B. ovatus has discrete PUL for MLG, GM, and GGM (11). RESULTS 24 52 carbohydrate-binding modules site Notably, the absence of carbohydrate-binding modules in the GHs encoded by the XyGUL implies that noncatalytic recognition of xyloglucan is mediated entirely by SGBP-A and -B. RESULTS 60 63 GHs protein_type Notably, the absence of carbohydrate-binding modules in the GHs encoded by the XyGUL implies that noncatalytic recognition of xyloglucan is mediated entirely by SGBP-A and -B. RESULTS 79 84 XyGUL gene Notably, the absence of carbohydrate-binding modules in the GHs encoded by the XyGUL implies that noncatalytic recognition of xyloglucan is mediated entirely by SGBP-A and -B. RESULTS 126 136 xyloglucan chemical Notably, the absence of carbohydrate-binding modules in the GHs encoded by the XyGUL implies that noncatalytic recognition of xyloglucan is mediated entirely by SGBP-A and -B. RESULTS 161 167 SGBP-A protein Notably, the absence of carbohydrate-binding modules in the GHs encoded by the XyGUL implies that noncatalytic recognition of xyloglucan is mediated entirely by SGBP-A and -B. RESULTS 172 174 -B protein Notably, the absence of carbohydrate-binding modules in the GHs encoded by the XyGUL implies that noncatalytic recognition of xyloglucan is mediated entirely by SGBP-A and -B. RESULTS 0 6 SGBP-A protein SGBP-A and SGBP-B preferentially bind xyloglucan. FIG 11 17 SGBP-B protein SGBP-A and SGBP-B preferentially bind xyloglucan. FIG 38 48 xyloglucan chemical SGBP-A and SGBP-B preferentially bind xyloglucan. FIG 0 24 Affinity electrophoresis experimental_method Affinity electrophoresis (10% acrylamide) of SGBP-A and SGBP-B with BSA as a control protein. FIG 45 51 SGBP-A protein Affinity electrophoresis (10% acrylamide) of SGBP-A and SGBP-B with BSA as a control protein. FIG 56 62 SGBP-B protein Affinity electrophoresis (10% acrylamide) of SGBP-A and SGBP-B with BSA as a control protein. FIG 68 71 BSA protein Affinity electrophoresis (10% acrylamide) of SGBP-A and SGBP-B with BSA as a control protein. FIG 52 55 BSA protein All samples were loaded on the same gel next to the BSA controls; thin black lines indicate where intervening lanes were removed from the final image for both space and clarity. FIG 18 32 polysaccharide chemical The percentage of polysaccharide incorporated into each native gel is displayed. FIG 13 31 endo-xyloglucanase protein_type The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 39 44 XyGUL gene The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 46 51 BoGH5 protein The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 80 94 polysaccharide chemical The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 109 117 glucosyl chemical The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 139 165 xylogluco-oligosaccharides chemical The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 167 172 XyGOs chemical The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 187 200 Glc4 backbone structure_element The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 206 241 variable side-chain galactosylation structure_element The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 243 248 XyGO1 chemical The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 312 350 controlled digestion and fractionation experimental_method The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 354 383 size exclusion chromatography experimental_method The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 421 437 oligosaccharides chemical The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 445 450 XyGO2 chemical The vanguard endo-xyloglucanase of the XyGUL, BoGH5, preferentially cleaves the polysaccharide at unbranched glucosyl residues to generate xylogluco-oligosaccharides (XyGOs) comprising a Glc4 backbone with variable side-chain galactosylation (XyGO1) (Fig. 1A; n = 1) as the limit of digestion products in vitro; controlled digestion and fractionation by size exclusion chromatography allow the production of higher-order oligosaccharides (e.g., XyGO2) (Fig. 1A; n = 2). RESULTS 0 3 ITC experimental_method ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 22 28 SGBP-A protein ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 38 41 XyG chemical ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 42 56 polysaccharide chemical ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 61 66 XyGO2 chemical ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 79 92 Glc8 backbone structure_element ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 117 127 affinities evidence ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 149 154 XyGO1 chemical ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 156 169 Glc4 backbone structure_element ITC demonstrates that SGBP-A binds to XyG polysaccharide and XyGO2 (based on a Glc8 backbone) with essentially equal affinities, while no binding of XyGO1 (Glc4 backbone) was detectable (Table 1; see Fig. S2 and S3 in the supplemental material). RESULTS 11 17 SGBP-B protein Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 23 31 bound to protein_state Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 32 35 XyG chemical Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 40 45 XyGO2 chemical Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 71 81 affinities evidence Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 107 109 Ka evidence Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 158 164 SGBP-A protein Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 186 192 SGBP-A protein Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 194 200 SGBP-B protein Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 206 214 bound to protein_state Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 215 220 XyGO1 chemical Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 230 238 affinity evidence Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 248 270 minimal repeating unit structure_element Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 288 290 Ka evidence Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 340 343 XyG chemical Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 348 353 XyGO2 chemical Similarly, SGBP-B also bound to XyG and XyGO2 with approximately equal affinities, although in both cases, Ka values were nearly 10-fold lower than those for SGBP-A. Also in contrast to SGBP-A, SGBP-B also bound to XyGO1, yet the affinity for this minimal repeating unit was poor, with a Ka value of ca. 1 order of magnitude lower than for XyG and XyGO2. RESULTS 42 56 polysaccharide chemical Together, these data clearly suggest that polysaccharide binding of both SGBPs is fulfilled by a dimer of the minimal repeat, corresponding to XyGO2 (cf. RESULTS 73 78 SGBPs protein_type Together, these data clearly suggest that polysaccharide binding of both SGBPs is fulfilled by a dimer of the minimal repeat, corresponding to XyGO2 (cf. RESULTS 97 102 dimer oligomeric_state Together, these data clearly suggest that polysaccharide binding of both SGBPs is fulfilled by a dimer of the minimal repeat, corresponding to XyGO2 (cf. RESULTS 110 124 minimal repeat structure_element Together, these data clearly suggest that polysaccharide binding of both SGBPs is fulfilled by a dimer of the minimal repeat, corresponding to XyGO2 (cf. RESULTS 143 148 XyGO2 chemical Together, these data clearly suggest that polysaccharide binding of both SGBPs is fulfilled by a dimer of the minimal repeat, corresponding to XyGO2 (cf. RESULTS 19 32 affinity PAGE experimental_method The observation by affinity PAGE that these proteins specifically recognize XyG is further substantiated by their lack of binding for the undecorated oligosaccharide cellotetraose (Table 1; see Fig. S3). RESULTS 76 79 XyG chemical The observation by affinity PAGE that these proteins specifically recognize XyG is further substantiated by their lack of binding for the undecorated oligosaccharide cellotetraose (Table 1; see Fig. S3). RESULTS 150 165 oligosaccharide chemical The observation by affinity PAGE that these proteins specifically recognize XyG is further substantiated by their lack of binding for the undecorated oligosaccharide cellotetraose (Table 1; see Fig. S3). RESULTS 166 179 cellotetraose chemical The observation by affinity PAGE that these proteins specifically recognize XyG is further substantiated by their lack of binding for the undecorated oligosaccharide cellotetraose (Table 1; see Fig. S3). RESULTS 13 19 SGBP-A protein Furthermore, SGBP-A binds cellohexaose with ~770-fold weaker affinity than XyG, while SGBP-B displays no detectable binding to this linear hexasaccharide. RESULTS 26 38 cellohexaose chemical Furthermore, SGBP-A binds cellohexaose with ~770-fold weaker affinity than XyG, while SGBP-B displays no detectable binding to this linear hexasaccharide. RESULTS 61 69 affinity evidence Furthermore, SGBP-A binds cellohexaose with ~770-fold weaker affinity than XyG, while SGBP-B displays no detectable binding to this linear hexasaccharide. RESULTS 75 78 XyG chemical Furthermore, SGBP-A binds cellohexaose with ~770-fold weaker affinity than XyG, while SGBP-B displays no detectable binding to this linear hexasaccharide. RESULTS 86 92 SGBP-B protein Furthermore, SGBP-A binds cellohexaose with ~770-fold weaker affinity than XyG, while SGBP-B displays no detectable binding to this linear hexasaccharide. RESULTS 139 153 hexasaccharide chemical Furthermore, SGBP-A binds cellohexaose with ~770-fold weaker affinity than XyG, while SGBP-B displays no detectable binding to this linear hexasaccharide. RESULTS 48 53 XyGUL gene To provide molecular-level insight into how the XyGUL SGBPs equip B. ovatus to specifically harvest XyG from the gut environment, we performed X-ray crystallography analysis of both SGBP-A and SGPB-B in oligosaccharide-complex forms. RESULTS 54 59 SGBPs protein_type To provide molecular-level insight into how the XyGUL SGBPs equip B. ovatus to specifically harvest XyG from the gut environment, we performed X-ray crystallography analysis of both SGBP-A and SGPB-B in oligosaccharide-complex forms. RESULTS 66 75 B. ovatus species To provide molecular-level insight into how the XyGUL SGBPs equip B. ovatus to specifically harvest XyG from the gut environment, we performed X-ray crystallography analysis of both SGBP-A and SGPB-B in oligosaccharide-complex forms. RESULTS 100 103 XyG chemical To provide molecular-level insight into how the XyGUL SGBPs equip B. ovatus to specifically harvest XyG from the gut environment, we performed X-ray crystallography analysis of both SGBP-A and SGPB-B in oligosaccharide-complex forms. RESULTS 143 164 X-ray crystallography experimental_method To provide molecular-level insight into how the XyGUL SGBPs equip B. ovatus to specifically harvest XyG from the gut environment, we performed X-ray crystallography analysis of both SGBP-A and SGPB-B in oligosaccharide-complex forms. RESULTS 182 188 SGBP-A protein To provide molecular-level insight into how the XyGUL SGBPs equip B. ovatus to specifically harvest XyG from the gut environment, we performed X-ray crystallography analysis of both SGBP-A and SGPB-B in oligosaccharide-complex forms. RESULTS 193 199 SGPB-B protein To provide molecular-level insight into how the XyGUL SGBPs equip B. ovatus to specifically harvest XyG from the gut environment, we performed X-ray crystallography analysis of both SGBP-A and SGPB-B in oligosaccharide-complex forms. RESULTS 203 232 oligosaccharide-complex forms complex_assembly To provide molecular-level insight into how the XyGUL SGBPs equip B. ovatus to specifically harvest XyG from the gut environment, we performed X-ray crystallography analysis of both SGBP-A and SGPB-B in oligosaccharide-complex forms. RESULTS 40 49 wild-type protein_state Summary of thermodynamic parameters for wild-type SGBP-A and SGBP-B obtained by isothermal titration calorimetry at 25°Ca TABLE 50 56 SGBP-A protein Summary of thermodynamic parameters for wild-type SGBP-A and SGBP-B obtained by isothermal titration calorimetry at 25°Ca TABLE 61 67 SGBP-B protein Summary of thermodynamic parameters for wild-type SGBP-A and SGBP-B obtained by isothermal titration calorimetry at 25°Ca TABLE 80 112 isothermal titration calorimetry experimental_method Summary of thermodynamic parameters for wild-type SGBP-A and SGBP-B obtained by isothermal titration calorimetry at 25°Ca TABLE 0 6 SGBP-A protein SGBP-A is a SusD homolog with an extensive glycan-binding platform. RESULTS 12 16 SusD protein SGBP-A is a SusD homolog with an extensive glycan-binding platform. RESULTS 43 66 glycan-binding platform site SGBP-A is a SusD homolog with an extensive glycan-binding platform. RESULTS 68 77 structure evidence As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 81 84 apo protein_state As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 85 91 SGBP-A protein As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 101 106 Rwork evidence As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 116 121 Rfree evidence As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 140 149 28 to 546 residue_range As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 184 208 “SusD-like” protein fold structure_element As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 227 252 tetratrico-peptide repeat structure_element As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 254 257 TPR structure_element As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 294 303 structure evidence As anticipated by sequence similarity, the high-resolution tertiary structure of apo-SGBP-A (1.36 Å, Rwork = 14.7%, Rfree = 17.4%, residues 28 to 546) (Table 2) displays the canonical “SusD-like” protein fold dominated by four tetratrico-peptide repeat (TPR) motifs that cradle the rest of the structure (Fig. 4A). RESULTS 14 20 SGBP-A protein Specifically, SGBP-A overlays B. thetaiotaomicron SusD (BtSusD) with a root mean square deviation (RMSD) value of 2.2 Å for 363 Cα pairs, which is notable given the 26% amino acid identity (40% similarity) between these homologs (Fig. 4C). RESULTS 21 29 overlays experimental_method Specifically, SGBP-A overlays B. thetaiotaomicron SusD (BtSusD) with a root mean square deviation (RMSD) value of 2.2 Å for 363 Cα pairs, which is notable given the 26% amino acid identity (40% similarity) between these homologs (Fig. 4C). RESULTS 30 49 B. thetaiotaomicron species Specifically, SGBP-A overlays B. thetaiotaomicron SusD (BtSusD) with a root mean square deviation (RMSD) value of 2.2 Å for 363 Cα pairs, which is notable given the 26% amino acid identity (40% similarity) between these homologs (Fig. 4C). RESULTS 50 54 SusD protein Specifically, SGBP-A overlays B. thetaiotaomicron SusD (BtSusD) with a root mean square deviation (RMSD) value of 2.2 Å for 363 Cα pairs, which is notable given the 26% amino acid identity (40% similarity) between these homologs (Fig. 4C). RESULTS 56 62 BtSusD protein Specifically, SGBP-A overlays B. thetaiotaomicron SusD (BtSusD) with a root mean square deviation (RMSD) value of 2.2 Å for 363 Cα pairs, which is notable given the 26% amino acid identity (40% similarity) between these homologs (Fig. 4C). RESULTS 71 97 root mean square deviation evidence Specifically, SGBP-A overlays B. thetaiotaomicron SusD (BtSusD) with a root mean square deviation (RMSD) value of 2.2 Å for 363 Cα pairs, which is notable given the 26% amino acid identity (40% similarity) between these homologs (Fig. 4C). RESULTS 99 103 RMSD evidence Specifically, SGBP-A overlays B. thetaiotaomicron SusD (BtSusD) with a root mean square deviation (RMSD) value of 2.2 Å for 363 Cα pairs, which is notable given the 26% amino acid identity (40% similarity) between these homologs (Fig. 4C). RESULTS 0 17 Cocrystallization experimental_method Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 21 27 SGBP-A protein Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 33 38 XyGO2 chemical Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 51 68 substrate complex complex_assembly Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 69 78 structure evidence Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 87 92 Rwork evidence Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 102 107 Rfree evidence Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 126 135 36 to 546 residue_range Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 189 201 binding-site site Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 222 241 XyG binding protein protein_type Cocrystallization of SGBP-A with XyGO2 generated a substrate complex structure (2.3 Å, Rwork = 21.8%, Rfree = 24.8%, residues 36 to 546) (Fig. 4A and B; Table 2) that revealed the distinct binding-site architecture of the XyG binding protein. RESULTS 4 16 SGBP-A:XyGO2 complex_assembly The SGBP-A:XyGO2 complex superimposes closely with the apo structure (RMSD of 0.6 Å) and demonstrates that no major conformational change occurs upon substrate binding; small deviations in the orientation of several surface loops are likely the result of differential crystal packing. RESULTS 25 37 superimposes experimental_method The SGBP-A:XyGO2 complex superimposes closely with the apo structure (RMSD of 0.6 Å) and demonstrates that no major conformational change occurs upon substrate binding; small deviations in the orientation of several surface loops are likely the result of differential crystal packing. RESULTS 55 58 apo protein_state The SGBP-A:XyGO2 complex superimposes closely with the apo structure (RMSD of 0.6 Å) and demonstrates that no major conformational change occurs upon substrate binding; small deviations in the orientation of several surface loops are likely the result of differential crystal packing. RESULTS 59 68 structure evidence The SGBP-A:XyGO2 complex superimposes closely with the apo structure (RMSD of 0.6 Å) and demonstrates that no major conformational change occurs upon substrate binding; small deviations in the orientation of several surface loops are likely the result of differential crystal packing. RESULTS 70 74 RMSD evidence The SGBP-A:XyGO2 complex superimposes closely with the apo structure (RMSD of 0.6 Å) and demonstrates that no major conformational change occurs upon substrate binding; small deviations in the orientation of several surface loops are likely the result of differential crystal packing. RESULTS 61 80 ligand-binding site site It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 84 93 conserved protein_state It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 102 108 SGBP-A protein It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 113 117 SusD protein It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 127 133 SGBP-A protein It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 157 174 aromatic platform site It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 211 214 XyG chemical It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 252 255 XyG chemical It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 310 314 site site It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 322 326 SusD protein It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 372 379 amylose chemical It is particularly notable that although the location of the ligand-binding site is conserved between SGBP-A and SusD, that of SGBP-A displays an ~29-Å-long aromatic platform to accommodate the extended, linear XyG chain (see reference for a review of XyG secondary structure), versus the shorter, ~18-Å-long, site within SusD that complements the helical conformation of amylose (Fig. 4C and D). RESULTS 10 19 structure evidence Molecular structure of SGBP-A (Bacova_02651). (A) Overlay of SGBP-A from the apo (rainbow) and XyGO2 (gray) structures. FIG 23 29 SGBP-A protein Molecular structure of SGBP-A (Bacova_02651). (A) Overlay of SGBP-A from the apo (rainbow) and XyGO2 (gray) structures. FIG 31 43 Bacova_02651 gene Molecular structure of SGBP-A (Bacova_02651). (A) Overlay of SGBP-A from the apo (rainbow) and XyGO2 (gray) structures. FIG 50 57 Overlay experimental_method Molecular structure of SGBP-A (Bacova_02651). (A) Overlay of SGBP-A from the apo (rainbow) and XyGO2 (gray) structures. FIG 61 67 SGBP-A protein Molecular structure of SGBP-A (Bacova_02651). (A) Overlay of SGBP-A from the apo (rainbow) and XyGO2 (gray) structures. FIG 77 80 apo protein_state Molecular structure of SGBP-A (Bacova_02651). (A) Overlay of SGBP-A from the apo (rainbow) and XyGO2 (gray) structures. FIG 95 100 XyGO2 chemical Molecular structure of SGBP-A (Bacova_02651). (A) Overlay of SGBP-A from the apo (rainbow) and XyGO2 (gray) structures. FIG 108 118 structures evidence Molecular structure of SGBP-A (Bacova_02651). (A) Overlay of SGBP-A from the apo (rainbow) and XyGO2 (gray) structures. FIG 4 7 apo protein_state The apo structure is color ramped from blue to red. FIG 8 17 structure evidence The apo structure is color ramped from blue to red. FIG 3 11 omit map evidence An omit map (2σ) for XyGO2 (orange and red sticks) is displayed. FIG 21 26 XyGO2 chemical An omit map (2σ) for XyGO2 (orange and red sticks) is displayed. FIG 25 33 omit map evidence (B) Close-up view of the omit map as in panel A, rotated 90° clockwise. FIG 4 11 Overlay experimental_method (C) Overlay of the Cα backbones of SGBP-A (black) with XyGO2 (orange and red spheres) and BtSusD (blue) with maltoheptaose (pink and red spheres), highlighting the conservation of the glycan-binding site location. FIG 35 41 SGBP-A protein (C) Overlay of the Cα backbones of SGBP-A (black) with XyGO2 (orange and red spheres) and BtSusD (blue) with maltoheptaose (pink and red spheres), highlighting the conservation of the glycan-binding site location. FIG 55 60 XyGO2 chemical (C) Overlay of the Cα backbones of SGBP-A (black) with XyGO2 (orange and red spheres) and BtSusD (blue) with maltoheptaose (pink and red spheres), highlighting the conservation of the glycan-binding site location. FIG 90 96 BtSusD protein (C) Overlay of the Cα backbones of SGBP-A (black) with XyGO2 (orange and red spheres) and BtSusD (blue) with maltoheptaose (pink and red spheres), highlighting the conservation of the glycan-binding site location. FIG 109 122 maltoheptaose chemical (C) Overlay of the Cα backbones of SGBP-A (black) with XyGO2 (orange and red spheres) and BtSusD (blue) with maltoheptaose (pink and red spheres), highlighting the conservation of the glycan-binding site location. FIG 184 203 glycan-binding site site (C) Overlay of the Cα backbones of SGBP-A (black) with XyGO2 (orange and red spheres) and BtSusD (blue) with maltoheptaose (pink and red spheres), highlighting the conservation of the glycan-binding site location. FIG 20 26 SGBP-A protein (D) Close-up of the SGBP-A (black and orange) and SusD (blue and pink) glycan-binding sites. FIG 50 54 SusD protein (D) Close-up of the SGBP-A (black and orange) and SusD (blue and pink) glycan-binding sites. FIG 71 91 glycan-binding sites site (D) Close-up of the SGBP-A (black and orange) and SusD (blue and pink) glycan-binding sites. FIG 31 50 glycan-binding site site The approximate length of each glycan-binding site is displayed, colored to match the protein structures. (E) Stereo view of the xyloglucan-binding site of SGBP-A, displaying all residues within 4 Å of the ligand. FIG 86 104 protein structures evidence The approximate length of each glycan-binding site is displayed, colored to match the protein structures. (E) Stereo view of the xyloglucan-binding site of SGBP-A, displaying all residues within 4 Å of the ligand. FIG 129 152 xyloglucan-binding site site The approximate length of each glycan-binding site is displayed, colored to match the protein structures. (E) Stereo view of the xyloglucan-binding site of SGBP-A, displaying all residues within 4 Å of the ligand. FIG 156 162 SGBP-A protein The approximate length of each glycan-binding site is displayed, colored to match the protein structures. (E) Stereo view of the xyloglucan-binding site of SGBP-A, displaying all residues within 4 Å of the ligand. FIG 13 20 glucose chemical The backbone glucose residues are numbered from the nonreducing end; xylose residues are labeled X1 and X2. FIG 69 75 xylose chemical The backbone glucose residues are numbered from the nonreducing end; xylose residues are labeled X1 and X2. FIG 97 99 X1 residue_name_number The backbone glucose residues are numbered from the nonreducing end; xylose residues are labeled X1 and X2. FIG 104 106 X2 residue_name_number The backbone glucose residues are numbered from the nonreducing end; xylose residues are labeled X1 and X2. FIG 28 36 glucosyl chemical Seven of the eight backbone glucosyl residues of XyGO2 could be convincingly modeled in the ligand electron density, and only two α(1→6)-linked xylosyl residues were observed (Fig. 4B; cf. RESULTS 49 54 XyGO2 chemical Seven of the eight backbone glucosyl residues of XyGO2 could be convincingly modeled in the ligand electron density, and only two α(1→6)-linked xylosyl residues were observed (Fig. 4B; cf. RESULTS 92 115 ligand electron density evidence Seven of the eight backbone glucosyl residues of XyGO2 could be convincingly modeled in the ligand electron density, and only two α(1→6)-linked xylosyl residues were observed (Fig. 4B; cf. RESULTS 130 151 α(1→6)-linked xylosyl chemical Seven of the eight backbone glucosyl residues of XyGO2 could be convincingly modeled in the ligand electron density, and only two α(1→6)-linked xylosyl residues were observed (Fig. 4B; cf. RESULTS 12 28 electron density evidence Indeed, the electron density for the ligand suggests some disorder, which may arise from multiple oligosaccharide orientations along the binding site. RESULTS 98 113 oligosaccharide chemical Indeed, the electron density for the ligand suggests some disorder, which may arise from multiple oligosaccharide orientations along the binding site. RESULTS 137 149 binding site site Indeed, the electron density for the ligand suggests some disorder, which may arise from multiple oligosaccharide orientations along the binding site. RESULTS 24 27 W82 residue_name_number Three aromatic residues—W82, W283, W306—comprise the flat platform that stacks along the naturally twisted β-glucan backbone (Fig. 4E). RESULTS 29 33 W283 residue_name_number Three aromatic residues—W82, W283, W306—comprise the flat platform that stacks along the naturally twisted β-glucan backbone (Fig. 4E). RESULTS 35 39 W306 residue_name_number Three aromatic residues—W82, W283, W306—comprise the flat platform that stacks along the naturally twisted β-glucan backbone (Fig. 4E). RESULTS 53 66 flat platform site Three aromatic residues—W82, W283, W306—comprise the flat platform that stacks along the naturally twisted β-glucan backbone (Fig. 4E). RESULTS 107 115 β-glucan chemical Three aromatic residues—W82, W283, W306—comprise the flat platform that stacks along the naturally twisted β-glucan backbone (Fig. 4E). RESULTS 34 42 platform site The functional importance of this platform is underscored by the observation that the W82A W283A W306A mutant of SGBP-A, designated SGBP-A*, is completely devoid of XyG affinity (Table 3; see Fig. S4 in the supplemental material). RESULTS 86 90 W82A mutant The functional importance of this platform is underscored by the observation that the W82A W283A W306A mutant of SGBP-A, designated SGBP-A*, is completely devoid of XyG affinity (Table 3; see Fig. S4 in the supplemental material). RESULTS 91 96 W283A mutant The functional importance of this platform is underscored by the observation that the W82A W283A W306A mutant of SGBP-A, designated SGBP-A*, is completely devoid of XyG affinity (Table 3; see Fig. S4 in the supplemental material). RESULTS 97 102 W306A mutant The functional importance of this platform is underscored by the observation that the W82A W283A W306A mutant of SGBP-A, designated SGBP-A*, is completely devoid of XyG affinity (Table 3; see Fig. S4 in the supplemental material). RESULTS 103 109 mutant protein_state The functional importance of this platform is underscored by the observation that the W82A W283A W306A mutant of SGBP-A, designated SGBP-A*, is completely devoid of XyG affinity (Table 3; see Fig. S4 in the supplemental material). RESULTS 113 119 SGBP-A protein The functional importance of this platform is underscored by the observation that the W82A W283A W306A mutant of SGBP-A, designated SGBP-A*, is completely devoid of XyG affinity (Table 3; see Fig. S4 in the supplemental material). RESULTS 132 139 SGBP-A* mutant The functional importance of this platform is underscored by the observation that the W82A W283A W306A mutant of SGBP-A, designated SGBP-A*, is completely devoid of XyG affinity (Table 3; see Fig. S4 in the supplemental material). RESULTS 144 177 completely devoid of XyG affinity protein_state The functional importance of this platform is underscored by the observation that the W82A W283A W306A mutant of SGBP-A, designated SGBP-A*, is completely devoid of XyG affinity (Table 3; see Fig. S4 in the supplemental material). RESULTS 77 81 W82A mutant Dissection of the individual contribution of these residues reveals that the W82A mutant displays a significant 4.9-fold decrease in the Ka value for XyG, while the W306A substitution completely abolishes XyG binding. RESULTS 82 88 mutant protein_state Dissection of the individual contribution of these residues reveals that the W82A mutant displays a significant 4.9-fold decrease in the Ka value for XyG, while the W306A substitution completely abolishes XyG binding. RESULTS 137 139 Ka evidence Dissection of the individual contribution of these residues reveals that the W82A mutant displays a significant 4.9-fold decrease in the Ka value for XyG, while the W306A substitution completely abolishes XyG binding. RESULTS 150 153 XyG chemical Dissection of the individual contribution of these residues reveals that the W82A mutant displays a significant 4.9-fold decrease in the Ka value for XyG, while the W306A substitution completely abolishes XyG binding. RESULTS 165 170 W306A mutant Dissection of the individual contribution of these residues reveals that the W82A mutant displays a significant 4.9-fold decrease in the Ka value for XyG, while the W306A substitution completely abolishes XyG binding. RESULTS 171 183 substitution experimental_method Dissection of the individual contribution of these residues reveals that the W82A mutant displays a significant 4.9-fold decrease in the Ka value for XyG, while the W306A substitution completely abolishes XyG binding. RESULTS 195 216 abolishes XyG binding protein_state Dissection of the individual contribution of these residues reveals that the W82A mutant displays a significant 4.9-fold decrease in the Ka value for XyG, while the W306A substitution completely abolishes XyG binding. RESULTS 137 143 ligand chemical Contrasting with the clear importance of these hydrophobic interactions, there are remarkably few hydrogen-bonding interactions with the ligand, which are provided by R65, N83, and S308, which are proximal to Glc5 and Glc3. RESULTS 167 170 R65 residue_name_number Contrasting with the clear importance of these hydrophobic interactions, there are remarkably few hydrogen-bonding interactions with the ligand, which are provided by R65, N83, and S308, which are proximal to Glc5 and Glc3. RESULTS 172 175 N83 residue_name_number Contrasting with the clear importance of these hydrophobic interactions, there are remarkably few hydrogen-bonding interactions with the ligand, which are provided by R65, N83, and S308, which are proximal to Glc5 and Glc3. RESULTS 181 185 S308 residue_name_number Contrasting with the clear importance of these hydrophobic interactions, there are remarkably few hydrogen-bonding interactions with the ligand, which are provided by R65, N83, and S308, which are proximal to Glc5 and Glc3. RESULTS 209 213 Glc5 residue_name_number Contrasting with the clear importance of these hydrophobic interactions, there are remarkably few hydrogen-bonding interactions with the ligand, which are provided by R65, N83, and S308, which are proximal to Glc5 and Glc3. RESULTS 218 222 Glc3 residue_name_number Contrasting with the clear importance of these hydrophobic interactions, there are remarkably few hydrogen-bonding interactions with the ligand, which are provided by R65, N83, and S308, which are proximal to Glc5 and Glc3. RESULTS 32 55 saccharide-binding data evidence Most surprising in light of the saccharide-binding data, however, was a lack of extensive recognition of the XyG side chains; only Y84 appeared to provide a hydrophobic interface for a xylosyl residue (Xyl1). RESULTS 109 112 XyG chemical Most surprising in light of the saccharide-binding data, however, was a lack of extensive recognition of the XyG side chains; only Y84 appeared to provide a hydrophobic interface for a xylosyl residue (Xyl1). RESULTS 131 134 Y84 residue_name_number Most surprising in light of the saccharide-binding data, however, was a lack of extensive recognition of the XyG side chains; only Y84 appeared to provide a hydrophobic interface for a xylosyl residue (Xyl1). RESULTS 157 178 hydrophobic interface site Most surprising in light of the saccharide-binding data, however, was a lack of extensive recognition of the XyG side chains; only Y84 appeared to provide a hydrophobic interface for a xylosyl residue (Xyl1). RESULTS 185 192 xylosyl chemical Most surprising in light of the saccharide-binding data, however, was a lack of extensive recognition of the XyG side chains; only Y84 appeared to provide a hydrophobic interface for a xylosyl residue (Xyl1). RESULTS 202 206 Xyl1 residue_name_number Most surprising in light of the saccharide-binding data, however, was a lack of extensive recognition of the XyG side chains; only Y84 appeared to provide a hydrophobic interface for a xylosyl residue (Xyl1). RESULTS 65 71 SGBP-A protein Summary of thermodynamic parameters for site-directed mutants of SGBP-A and SGBP-B obtained by ITC with XyG at 25°Ca TABLE 76 82 SGBP-B protein Summary of thermodynamic parameters for site-directed mutants of SGBP-A and SGBP-B obtained by ITC with XyG at 25°Ca TABLE 95 98 ITC experimental_method Summary of thermodynamic parameters for site-directed mutants of SGBP-A and SGBP-B obtained by ITC with XyG at 25°Ca TABLE 104 107 XyG chemical Summary of thermodynamic parameters for site-directed mutants of SGBP-A and SGBP-B obtained by ITC with XyG at 25°Ca TABLE 13 15 Ka evidence "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 34 36 ΔH evidence "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 52 55 TΔS evidence "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 92 98 SGBP-A protein "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 99 103 W82A mutant "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 104 109 W283A mutant "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 110 115 W306A mutant "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 134 140 SGBP-A protein "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 141 145 W82A mutant "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 178 184 SGBP-A protein "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 185 189 W306 residue_name_number "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 208 214 SGBP-B protein "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 215 222 230–489 residue_range "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 271 277 SGBP-B protein "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 278 283 Y363A mutant "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 334 340 SGBP-B protein "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 341 346 W364A mutant "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 373 379 SGBP-B protein "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 380 385 F414A mutant "Protein name Ka ΔG (kcal ⋅ mol−1) ΔH (kcal ⋅ mol−1) TΔS (kcal ⋅ mol−1) Fold changeb M−1 SGBP-A(W82A W283A W306A) ND NB NB NB NB SGBP-A(W82A)c 4.9 9.1 × 104 −6.8 −6.3 0.5 SGBP-A(W306) ND NB NB NB NB SGBP-B(230–489) 0.7 (8.6 ± 0.20) × 104 −6.7 −14.9 ± 0.1 −8.2 SGBP-B(Y363A) 19.7 (2.9 ± 0.10) × 103 −4.7 −18.1 ± 0.1 −13.3 SGBP-B(W364A) ND Weak Weak Weak Weak SGBP-B(F414A) 3.2 (1.80 ± 0.03) × 104 −5.8 −11.4 ± 0.1 −5.6 " TABLE 75 80 XyGO2 chemical Binding thermodynamics are based on the concentration of the binding unit, XyGO2. TABLE 26 28 Ka evidence Weak binding represents a Ka of <500 M−1. TABLE 0 2 Ka evidence Ka fold change = Ka of wild-type protein/Ka of mutant protein for xyloglucan binding. TABLE 17 19 Ka evidence Ka fold change = Ka of wild-type protein/Ka of mutant protein for xyloglucan binding. TABLE 23 32 wild-type protein_state Ka fold change = Ka of wild-type protein/Ka of mutant protein for xyloglucan binding. TABLE 41 43 Ka evidence Ka fold change = Ka of wild-type protein/Ka of mutant protein for xyloglucan binding. TABLE 66 76 xyloglucan chemical Ka fold change = Ka of wild-type protein/Ka of mutant protein for xyloglucan binding. TABLE 0 6 SGBP-B protein SGBP-B has a multimodular structure with a single, C-terminal glycan-binding domain. RESULTS 62 83 glycan-binding domain structure_element SGBP-B has a multimodular structure with a single, C-terminal glycan-binding domain. RESULTS 4 21 crystal structure evidence The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 25 36 full-length protein_state The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 37 43 SGBP-B protein The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 44 59 in complex with protein_state The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 60 65 XyGO2 chemical The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 75 80 Rwork evidence The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 90 95 Rfree evidence The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 114 123 34 to 489 residue_range The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 156 165 structure evidence The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 184 223 tandem immunoglobulin (Ig)-like domains structure_element The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 233 234 A structure_element The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 236 237 B structure_element The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 243 244 C structure_element The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 284 309 xyloglucan-binding domain structure_element The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 318 319 D structure_element The crystal structure of full-length SGBP-B in complex with XyGO2 (2.37 Å, Rwork = 19.9%, Rfree = 23.9%, residues 34 to 489) (Table 2) revealed an extended structure composed of three tandem immunoglobulin (Ig)-like domains (domains A, B, and C) followed at the C terminus by a novel xyloglucan-binding domain (domain D) (Fig. 5A). RESULTS 8 9 A structure_element Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 11 12 B structure_element Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 18 19 C structure_element Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 36 52 β-sandwich folds structure_element Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 62 63 B structure_element Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 74 84 134 to 230 residue_range Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 90 91 C structure_element Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 102 112 231 to 313 residue_range Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 121 133 superimposed experimental_method Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 146 147 A structure_element Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 158 167 34 to 133 residue_range Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 174 179 RMSDs evidence Domains A, B, and C display similar β-sandwich folds; domains B (residues 134 to 230) and C (residues 231 to 313) can be superimposed onto domain A (residues 34 to 133) with RMSDs of 1.1 and 1.2 Å, respectively, for 47 atom pairs (23% and 16% sequence identity, respectively). RESULTS 0 13 These domains structure_element These domains also display similarity to the C-terminal β-sandwich domains of many GH13 enzymes, including the cyclodextrin glucanotransferase of Geobacillus stearothermophilus (Fig. 5B). RESULTS 56 74 β-sandwich domains structure_element These domains also display similarity to the C-terminal β-sandwich domains of many GH13 enzymes, including the cyclodextrin glucanotransferase of Geobacillus stearothermophilus (Fig. 5B). RESULTS 83 95 GH13 enzymes protein_type These domains also display similarity to the C-terminal β-sandwich domains of many GH13 enzymes, including the cyclodextrin glucanotransferase of Geobacillus stearothermophilus (Fig. 5B). RESULTS 111 142 cyclodextrin glucanotransferase protein_type These domains also display similarity to the C-terminal β-sandwich domains of many GH13 enzymes, including the cyclodextrin glucanotransferase of Geobacillus stearothermophilus (Fig. 5B). RESULTS 146 176 Geobacillus stearothermophilus species These domains also display similarity to the C-terminal β-sandwich domains of many GH13 enzymes, including the cyclodextrin glucanotransferase of Geobacillus stearothermophilus (Fig. 5B). RESULTS 0 12 Such domains structure_element Such domains are not typically involved in carbohydrate binding. RESULTS 43 55 carbohydrate chemical Such domains are not typically involved in carbohydrate binding. RESULTS 8 25 visual inspection experimental_method Indeed, visual inspection of the SGBP-B structure, as well as individual production of the A and B domains and affinity PAGE analysis (see Fig. S5 in the supplemental material), indicates that these domains do not contribute to XyG capture. RESULTS 33 39 SGBP-B protein Indeed, visual inspection of the SGBP-B structure, as well as individual production of the A and B domains and affinity PAGE analysis (see Fig. S5 in the supplemental material), indicates that these domains do not contribute to XyG capture. RESULTS 40 49 structure evidence Indeed, visual inspection of the SGBP-B structure, as well as individual production of the A and B domains and affinity PAGE analysis (see Fig. S5 in the supplemental material), indicates that these domains do not contribute to XyG capture. RESULTS 91 92 A structure_element Indeed, visual inspection of the SGBP-B structure, as well as individual production of the A and B domains and affinity PAGE analysis (see Fig. S5 in the supplemental material), indicates that these domains do not contribute to XyG capture. RESULTS 97 98 B structure_element Indeed, visual inspection of the SGBP-B structure, as well as individual production of the A and B domains and affinity PAGE analysis (see Fig. S5 in the supplemental material), indicates that these domains do not contribute to XyG capture. RESULTS 111 124 affinity PAGE experimental_method Indeed, visual inspection of the SGBP-B structure, as well as individual production of the A and B domains and affinity PAGE analysis (see Fig. S5 in the supplemental material), indicates that these domains do not contribute to XyG capture. RESULTS 228 231 XyG chemical Indeed, visual inspection of the SGBP-B structure, as well as individual production of the A and B domains and affinity PAGE analysis (see Fig. S5 in the supplemental material), indicates that these domains do not contribute to XyG capture. RESULTS 19 29 production experimental_method On the other hand, production of the fused domains C and D in tandem (SGBP-B residues 230 to 489) retains complete binding of xyloglucan in vitro, with the observed slight increase in affinity likely arising from a reduced potential for steric hindrance of the smaller protein construct during polysaccharide interactions (Table 3). RESULTS 37 58 fused domains C and D mutant On the other hand, production of the fused domains C and D in tandem (SGBP-B residues 230 to 489) retains complete binding of xyloglucan in vitro, with the observed slight increase in affinity likely arising from a reduced potential for steric hindrance of the smaller protein construct during polysaccharide interactions (Table 3). RESULTS 70 76 SGBP-B protein On the other hand, production of the fused domains C and D in tandem (SGBP-B residues 230 to 489) retains complete binding of xyloglucan in vitro, with the observed slight increase in affinity likely arising from a reduced potential for steric hindrance of the smaller protein construct during polysaccharide interactions (Table 3). RESULTS 86 96 230 to 489 residue_range On the other hand, production of the fused domains C and D in tandem (SGBP-B residues 230 to 489) retains complete binding of xyloglucan in vitro, with the observed slight increase in affinity likely arising from a reduced potential for steric hindrance of the smaller protein construct during polysaccharide interactions (Table 3). RESULTS 126 136 xyloglucan chemical On the other hand, production of the fused domains C and D in tandem (SGBP-B residues 230 to 489) retains complete binding of xyloglucan in vitro, with the observed slight increase in affinity likely arising from a reduced potential for steric hindrance of the smaller protein construct during polysaccharide interactions (Table 3). RESULTS 294 308 polysaccharide chemical On the other hand, production of the fused domains C and D in tandem (SGBP-B residues 230 to 489) retains complete binding of xyloglucan in vitro, with the observed slight increase in affinity likely arising from a reduced potential for steric hindrance of the smaller protein construct during polysaccharide interactions (Table 3). RESULTS 18 29 full-length protein_state While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 49 50 D structure_element While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 89 109 XyG-binding proteins protein_type While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 127 133 SGBP-B protein While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 148 169 xylan-binding protein protein_type While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 170 182 Bacova_04391 protein While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 211 216 xylan chemical While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 227 230 PUL gene While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 234 243 B. ovatus species While neither the full-length protein nor domain D displays structural homology to known XyG-binding proteins, the topology of SGBP-B resembles the xylan-binding protein Bacova_04391 (PDB 3ORJ) encoded within a xylan-targeting PUL of B. ovatus (Fig. 5C). RESULTS 4 29 structure-based alignment experimental_method The structure-based alignment of these proteins reveals 17% sequence identity, with a core RMSD of 3.6 Å for 253 aligned residues. RESULTS 91 95 RMSD evidence The structure-based alignment of these proteins reveals 17% sequence identity, with a core RMSD of 3.6 Å for 253 aligned residues. RESULTS 51 63 Bacova_04391 protein While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 79 91 binding site site While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 116 120 W241 residue_name_number While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 125 129 Y404 residue_name_number While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 157 174 XyGO binding site site While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 178 184 SGBP-B protein While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 199 231 opposing, clamp-like arrangement protein_state While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 235 249 these residues structure_element While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 253 265 Bacova_04391 protein While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 295 321 planar surface arrangement site While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 329 337 residues structure_element While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 357 360 XyG chemical While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 364 370 SGBP-B protein While there is no substrate-complexed structure of Bacova_04391 available, the binding site is predicted to include W241 and Y404, which are proximal to the XyGO binding site in SGBP-B. However, the opposing, clamp-like arrangement of these residues in Bacova_04391 is clearly distinct from the planar surface arrangement of the residues that interact with XyG in SGBP-B (described below). RESULTS 26 32 SGBP-B protein Multimodular structure of SGBP-B (Bacova_02650). (A) Full-length structure of SGBP-B, color coded by domain as indicated. FIG 34 46 Bacova_02650 gene Multimodular structure of SGBP-B (Bacova_02650). (A) Full-length structure of SGBP-B, color coded by domain as indicated. FIG 53 64 Full-length protein_state Multimodular structure of SGBP-B (Bacova_02650). (A) Full-length structure of SGBP-B, color coded by domain as indicated. FIG 65 74 structure evidence Multimodular structure of SGBP-B (Bacova_02650). (A) Full-length structure of SGBP-B, color coded by domain as indicated. FIG 78 84 SGBP-B protein Multimodular structure of SGBP-B (Bacova_02650). (A) Full-length structure of SGBP-B, color coded by domain as indicated. FIG 0 8 Prolines residue_name Prolines between domains are indicated as spheres. FIG 3 11 omit map evidence An omit map (2σ) for XyGO2 is displayed to highlight the location of the glycan-binding site. FIG 21 26 XyGO2 chemical An omit map (2σ) for XyGO2 is displayed to highlight the location of the glycan-binding site. FIG 73 92 glycan-binding site site An omit map (2σ) for XyGO2 is displayed to highlight the location of the glycan-binding site. FIG 15 21 SGBP-B protein (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 30 31 A structure_element (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 33 34 B structure_element (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 40 41 C structure_element (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 85 99 Ig-like domain structure_element (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 107 128 G. stearothermophilus species (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 129 160 cyclodextrin glucanotransferase protein_type (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 181 191 375 to 493 residue_range (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 211 218 overlay experimental_method (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 222 228 SGBP-B protein (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 240 252 Bacova_04391 protein (B) Overlay of SGBP-B domains A, B, and C (colored as in panel A), with a C-terminal Ig-like domain of the G. stearothermophilus cyclodextrin glucanotransferase (PDB 1CYG [residues 375 to 493]) in green. (C) Cα overlay of SGBP-B (gray) and Bacova_04391 (PDB 3ORJ) (pink). FIG 13 21 omit map evidence (D) Close-up omit map for the XyGO2 ligand, contoured at 2σ. (E) Stereo view of the xyloglucan-binding site of SGBP-B, displaying all residues within 4 Å of the ligand. FIG 30 35 XyGO2 chemical (D) Close-up omit map for the XyGO2 ligand, contoured at 2σ. (E) Stereo view of the xyloglucan-binding site of SGBP-B, displaying all residues within 4 Å of the ligand. FIG 84 107 xyloglucan-binding site site (D) Close-up omit map for the XyGO2 ligand, contoured at 2σ. (E) Stereo view of the xyloglucan-binding site of SGBP-B, displaying all residues within 4 Å of the ligand. FIG 111 117 SGBP-B protein (D) Close-up omit map for the XyGO2 ligand, contoured at 2σ. (E) Stereo view of the xyloglucan-binding site of SGBP-B, displaying all residues within 4 Å of the ligand. FIG 13 20 glucose chemical The backbone glucose residues are numbered from the nonreducing end, xylose residues are shown as X1, X2, and X3, potential hydrogen-bonding interactions are shown as dashed lines, and the distance is shown in angstroms. FIG 69 75 xylose chemical The backbone glucose residues are numbered from the nonreducing end, xylose residues are shown as X1, X2, and X3, potential hydrogen-bonding interactions are shown as dashed lines, and the distance is shown in angstroms. FIG 98 100 X1 residue_name_number The backbone glucose residues are numbered from the nonreducing end, xylose residues are shown as X1, X2, and X3, potential hydrogen-bonding interactions are shown as dashed lines, and the distance is shown in angstroms. FIG 102 104 X2 residue_name_number The backbone glucose residues are numbered from the nonreducing end, xylose residues are shown as X1, X2, and X3, potential hydrogen-bonding interactions are shown as dashed lines, and the distance is shown in angstroms. FIG 110 112 X3 residue_name_number The backbone glucose residues are numbered from the nonreducing end, xylose residues are shown as X1, X2, and X3, potential hydrogen-bonding interactions are shown as dashed lines, and the distance is shown in angstroms. FIG 27 36 structure evidence Inspection of the tertiary structure indicates that domains C and D are effectively inseparable, with a contact interface of 396 Å2. RESULTS 60 61 C structure_element Inspection of the tertiary structure indicates that domains C and D are effectively inseparable, with a contact interface of 396 Å2. RESULTS 66 67 D structure_element Inspection of the tertiary structure indicates that domains C and D are effectively inseparable, with a contact interface of 396 Å2. RESULTS 8 9 A structure_element Domains A, B, and C do not pack against each other. RESULTS 11 12 B structure_element Domains A, B, and C do not pack against each other. RESULTS 18 19 C structure_element Domains A, B, and C do not pack against each other. RESULTS 14 34 five-residue linkers structure_element Moreover, the five-residue linkers between these first three domains all feature a proline as the middle residue, suggesting significant conformational rigidity (Fig. 5A). RESULTS 83 90 proline residue_name Moreover, the five-residue linkers between these first three domains all feature a proline as the middle residue, suggesting significant conformational rigidity (Fig. 5A). RESULTS 98 112 middle residue structure_element Moreover, the five-residue linkers between these first three domains all feature a proline as the middle residue, suggesting significant conformational rigidity (Fig. 5A). RESULTS 81 88 proline residue_name Despite the lack of sequence and structural conservation, a similarly positioned proline joins the Ig-like domains of the xylan-binding Bacova_04391 and the starch-binding proteins SusE and SusF. We speculate that this is a biologically important adaptation that serves to project the glycan binding site of these proteins far from the membrane surface. RESULTS 99 114 Ig-like domains structure_element Despite the lack of sequence and structural conservation, a similarly positioned proline joins the Ig-like domains of the xylan-binding Bacova_04391 and the starch-binding proteins SusE and SusF. We speculate that this is a biologically important adaptation that serves to project the glycan binding site of these proteins far from the membrane surface. RESULTS 136 148 Bacova_04391 protein Despite the lack of sequence and structural conservation, a similarly positioned proline joins the Ig-like domains of the xylan-binding Bacova_04391 and the starch-binding proteins SusE and SusF. We speculate that this is a biologically important adaptation that serves to project the glycan binding site of these proteins far from the membrane surface. RESULTS 157 180 starch-binding proteins protein_type Despite the lack of sequence and structural conservation, a similarly positioned proline joins the Ig-like domains of the xylan-binding Bacova_04391 and the starch-binding proteins SusE and SusF. We speculate that this is a biologically important adaptation that serves to project the glycan binding site of these proteins far from the membrane surface. RESULTS 181 185 SusE protein Despite the lack of sequence and structural conservation, a similarly positioned proline joins the Ig-like domains of the xylan-binding Bacova_04391 and the starch-binding proteins SusE and SusF. We speculate that this is a biologically important adaptation that serves to project the glycan binding site of these proteins far from the membrane surface. RESULTS 190 194 SusF protein Despite the lack of sequence and structural conservation, a similarly positioned proline joins the Ig-like domains of the xylan-binding Bacova_04391 and the starch-binding proteins SusE and SusF. We speculate that this is a biologically important adaptation that serves to project the glycan binding site of these proteins far from the membrane surface. RESULTS 285 304 glycan binding site site Despite the lack of sequence and structural conservation, a similarly positioned proline joins the Ig-like domains of the xylan-binding Bacova_04391 and the starch-binding proteins SusE and SusF. We speculate that this is a biologically important adaptation that serves to project the glycan binding site of these proteins far from the membrane surface. RESULTS 16 22 SGBP-B protein Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 123 143 eight-residue linker structure_element Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 169 178 lipidated protein_state Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 179 182 Cys residue_name Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 184 187 C28 residue_name_number Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 197 211 first β-strand structure_element Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 222 223 A structure_element Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 231 254 outer membrane proteins protein_type Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 268 284 Sus-like systems complex_assembly Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 303 339 10- to 20-amino-acid flexible linker structure_element Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 352 361 lipidated protein_state Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 362 365 Cys residue_name Any mobility of SGBP-B on the surface of the cell (beyond lateral diffusion within the membrane) is likely imparted by the eight-residue linker that spans the predicted lipidated Cys (C28) and the first β-strand of domain A. Other outer membrane proteins from various Sus-like systems possess a similar 10- to 20-amino-acid flexible linker between the lipidated Cys that tethers the protein to the outside the cell and the first secondary structure element. RESULTS 17 40 outer membrane-anchored protein_state Analogously, the outer membrane-anchored endo-xyloglucanase BoGH5 of the XyGUL contains a 100-amino-acid, all-β-strand, N-terminal module and flexible linker that imparts conformational flexibility and distances the catalytic module from the cell surface. RESULTS 41 59 endo-xyloglucanase protein_type Analogously, the outer membrane-anchored endo-xyloglucanase BoGH5 of the XyGUL contains a 100-amino-acid, all-β-strand, N-terminal module and flexible linker that imparts conformational flexibility and distances the catalytic module from the cell surface. RESULTS 60 65 BoGH5 protein Analogously, the outer membrane-anchored endo-xyloglucanase BoGH5 of the XyGUL contains a 100-amino-acid, all-β-strand, N-terminal module and flexible linker that imparts conformational flexibility and distances the catalytic module from the cell surface. RESULTS 73 78 XyGUL gene Analogously, the outer membrane-anchored endo-xyloglucanase BoGH5 of the XyGUL contains a 100-amino-acid, all-β-strand, N-terminal module and flexible linker that imparts conformational flexibility and distances the catalytic module from the cell surface. RESULTS 90 118 100-amino-acid, all-β-strand structure_element Analogously, the outer membrane-anchored endo-xyloglucanase BoGH5 of the XyGUL contains a 100-amino-acid, all-β-strand, N-terminal module and flexible linker that imparts conformational flexibility and distances the catalytic module from the cell surface. RESULTS 120 137 N-terminal module structure_element Analogously, the outer membrane-anchored endo-xyloglucanase BoGH5 of the XyGUL contains a 100-amino-acid, all-β-strand, N-terminal module and flexible linker that imparts conformational flexibility and distances the catalytic module from the cell surface. RESULTS 142 157 flexible linker structure_element Analogously, the outer membrane-anchored endo-xyloglucanase BoGH5 of the XyGUL contains a 100-amino-acid, all-β-strand, N-terminal module and flexible linker that imparts conformational flexibility and distances the catalytic module from the cell surface. RESULTS 216 232 catalytic module structure_element Analogously, the outer membrane-anchored endo-xyloglucanase BoGH5 of the XyGUL contains a 100-amino-acid, all-β-strand, N-terminal module and flexible linker that imparts conformational flexibility and distances the catalytic module from the cell surface. RESULTS 0 3 XyG chemical XyG binds to domain D of SGBP-B at the concave interface of the top β-sheet, with binding mediated by loops connecting the β-strands. RESULTS 4 12 binds to protein_state XyG binds to domain D of SGBP-B at the concave interface of the top β-sheet, with binding mediated by loops connecting the β-strands. RESULTS 20 21 D structure_element XyG binds to domain D of SGBP-B at the concave interface of the top β-sheet, with binding mediated by loops connecting the β-strands. RESULTS 25 31 SGBP-B protein XyG binds to domain D of SGBP-B at the concave interface of the top β-sheet, with binding mediated by loops connecting the β-strands. RESULTS 39 56 concave interface site XyG binds to domain D of SGBP-B at the concave interface of the top β-sheet, with binding mediated by loops connecting the β-strands. RESULTS 68 75 β-sheet structure_element XyG binds to domain D of SGBP-B at the concave interface of the top β-sheet, with binding mediated by loops connecting the β-strands. RESULTS 102 107 loops structure_element XyG binds to domain D of SGBP-B at the concave interface of the top β-sheet, with binding mediated by loops connecting the β-strands. RESULTS 123 132 β-strands structure_element XyG binds to domain D of SGBP-B at the concave interface of the top β-sheet, with binding mediated by loops connecting the β-strands. RESULTS 4 12 glucosyl chemical Six glucosyl residues, comprising the main chain, and three branching xylosyl residues of XyGO2 can be modeled in the density (Fig. 5D; cf. RESULTS 70 77 xylosyl chemical Six glucosyl residues, comprising the main chain, and three branching xylosyl residues of XyGO2 can be modeled in the density (Fig. 5D; cf. RESULTS 90 95 XyGO2 chemical Six glucosyl residues, comprising the main chain, and three branching xylosyl residues of XyGO2 can be modeled in the density (Fig. 5D; cf. RESULTS 118 125 density evidence Six glucosyl residues, comprising the main chain, and three branching xylosyl residues of XyGO2 can be modeled in the density (Fig. 5D; cf. RESULTS 82 119 cello- and xylogluco-oligosaccharides chemical The backbone is flat, with less of the “twisted-ribbon” geometry observed in some cello- and xylogluco-oligosaccharides. RESULTS 4 21 aromatic platform site The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 33 37 W330 residue_name_number The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 39 43 W364 residue_name_number The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 49 53 Y363 residue_name_number The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 65 73 glucosyl chemical The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 100 106 longer protein_state The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 107 115 platform site The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 119 125 SGBP-A protein The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 146 154 glucosyl chemical The aromatic platform created by W330, W364, and Y363 spans four glucosyl residues, compared to the longer platform of SGBP-A, which supports six glucosyl residues (Fig. 5E). RESULTS 4 9 Y363A mutant The Y363A site-directed mutant of SGBP-B displays a 20-fold decrease in the Ka for XyG, while the W364A mutant lacks XyG binding (Table 3; see Fig. S6 in the supplemental material). RESULTS 10 30 site-directed mutant experimental_method The Y363A site-directed mutant of SGBP-B displays a 20-fold decrease in the Ka for XyG, while the W364A mutant lacks XyG binding (Table 3; see Fig. S6 in the supplemental material). RESULTS 34 40 SGBP-B protein The Y363A site-directed mutant of SGBP-B displays a 20-fold decrease in the Ka for XyG, while the W364A mutant lacks XyG binding (Table 3; see Fig. S6 in the supplemental material). RESULTS 76 78 Ka evidence The Y363A site-directed mutant of SGBP-B displays a 20-fold decrease in the Ka for XyG, while the W364A mutant lacks XyG binding (Table 3; see Fig. S6 in the supplemental material). RESULTS 83 86 XyG chemical The Y363A site-directed mutant of SGBP-B displays a 20-fold decrease in the Ka for XyG, while the W364A mutant lacks XyG binding (Table 3; see Fig. S6 in the supplemental material). RESULTS 98 103 W364A mutant The Y363A site-directed mutant of SGBP-B displays a 20-fold decrease in the Ka for XyG, while the W364A mutant lacks XyG binding (Table 3; see Fig. S6 in the supplemental material). RESULTS 104 110 mutant protein_state The Y363A site-directed mutant of SGBP-B displays a 20-fold decrease in the Ka for XyG, while the W364A mutant lacks XyG binding (Table 3; see Fig. S6 in the supplemental material). RESULTS 111 128 lacks XyG binding protein_state The Y363A site-directed mutant of SGBP-B displays a 20-fold decrease in the Ka for XyG, while the W364A mutant lacks XyG binding (Table 3; see Fig. S6 in the supplemental material). RESULTS 61 69 β-glucan chemical There are no additional contacts between the protein and the β-glucan backbone and surprisingly few interactions with the side-chain xylosyl residues, despite that fact that ITC data demonstrate that SGBP-B does not measurably bind the cellohexaose (Table 1). RESULTS 133 140 xylosyl chemical There are no additional contacts between the protein and the β-glucan backbone and surprisingly few interactions with the side-chain xylosyl residues, despite that fact that ITC data demonstrate that SGBP-B does not measurably bind the cellohexaose (Table 1). RESULTS 174 177 ITC experimental_method There are no additional contacts between the protein and the β-glucan backbone and surprisingly few interactions with the side-chain xylosyl residues, despite that fact that ITC data demonstrate that SGBP-B does not measurably bind the cellohexaose (Table 1). RESULTS 200 206 SGBP-B protein There are no additional contacts between the protein and the β-glucan backbone and surprisingly few interactions with the side-chain xylosyl residues, despite that fact that ITC data demonstrate that SGBP-B does not measurably bind the cellohexaose (Table 1). RESULTS 236 248 cellohexaose chemical There are no additional contacts between the protein and the β-glucan backbone and surprisingly few interactions with the side-chain xylosyl residues, despite that fact that ITC data demonstrate that SGBP-B does not measurably bind the cellohexaose (Table 1). RESULTS 0 4 F414 residue_name_number F414 stacks with the xylosyl residue of Glc3, while Q407 is positioned for hydrogen bonding with the O4 of xylosyl residue Xyl1. RESULTS 21 28 xylosyl chemical F414 stacks with the xylosyl residue of Glc3, while Q407 is positioned for hydrogen bonding with the O4 of xylosyl residue Xyl1. RESULTS 40 44 Glc3 residue_name_number F414 stacks with the xylosyl residue of Glc3, while Q407 is positioned for hydrogen bonding with the O4 of xylosyl residue Xyl1. RESULTS 52 56 Q407 residue_name_number F414 stacks with the xylosyl residue of Glc3, while Q407 is positioned for hydrogen bonding with the O4 of xylosyl residue Xyl1. RESULTS 107 114 xylosyl chemical F414 stacks with the xylosyl residue of Glc3, while Q407 is positioned for hydrogen bonding with the O4 of xylosyl residue Xyl1. RESULTS 123 127 Xyl1 residue_name_number F414 stacks with the xylosyl residue of Glc3, while Q407 is positioned for hydrogen bonding with the O4 of xylosyl residue Xyl1. RESULTS 17 22 F414A mutant Surprisingly, an F414A mutant of SGBP-B displays only a mild 3-fold decrease in the Ka value for XyG, again suggesting that glycan recognition is primarily mediated via contact with the β-glucan backbone (Table 3; see Fig. S6). RESULTS 23 29 mutant protein_state Surprisingly, an F414A mutant of SGBP-B displays only a mild 3-fold decrease in the Ka value for XyG, again suggesting that glycan recognition is primarily mediated via contact with the β-glucan backbone (Table 3; see Fig. S6). RESULTS 33 39 SGBP-B protein Surprisingly, an F414A mutant of SGBP-B displays only a mild 3-fold decrease in the Ka value for XyG, again suggesting that glycan recognition is primarily mediated via contact with the β-glucan backbone (Table 3; see Fig. S6). RESULTS 84 86 Ka evidence Surprisingly, an F414A mutant of SGBP-B displays only a mild 3-fold decrease in the Ka value for XyG, again suggesting that glycan recognition is primarily mediated via contact with the β-glucan backbone (Table 3; see Fig. S6). RESULTS 97 100 XyG chemical Surprisingly, an F414A mutant of SGBP-B displays only a mild 3-fold decrease in the Ka value for XyG, again suggesting that glycan recognition is primarily mediated via contact with the β-glucan backbone (Table 3; see Fig. S6). RESULTS 124 130 glycan chemical Surprisingly, an F414A mutant of SGBP-B displays only a mild 3-fold decrease in the Ka value for XyG, again suggesting that glycan recognition is primarily mediated via contact with the β-glucan backbone (Table 3; see Fig. S6). RESULTS 11 19 residues structure_element Additional residues surrounding the binding site, including Y369 and E412, may contribute to the recognition of more highly decorated XyG, but precisely how this is mediated is presently unclear. RESULTS 36 48 binding site site Additional residues surrounding the binding site, including Y369 and E412, may contribute to the recognition of more highly decorated XyG, but precisely how this is mediated is presently unclear. RESULTS 60 64 Y369 residue_name_number Additional residues surrounding the binding site, including Y369 and E412, may contribute to the recognition of more highly decorated XyG, but precisely how this is mediated is presently unclear. RESULTS 69 73 E412 residue_name_number Additional residues surrounding the binding site, including Y369 and E412, may contribute to the recognition of more highly decorated XyG, but precisely how this is mediated is presently unclear. RESULTS 134 137 XyG chemical Additional residues surrounding the binding site, including Y369 and E412, may contribute to the recognition of more highly decorated XyG, but precisely how this is mediated is presently unclear. RESULTS 50 56 SGBP-B protein Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 57 67 xyloglucan chemical Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 84 90 solved experimental_method Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 95 112 crystal structure evidence Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 120 136 fused CD domains mutant Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 137 152 in complex with protein_state Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 153 158 XyGO2 chemical Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 168 173 Rwork evidence Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 183 188 Rfree evidence Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 207 217 230 to 489 residue_range Hoping to achieve a higher-resolution view of the SGBP-B–xyloglucan interaction, we solved the crystal structure of the fused CD domains in complex with XyGO2 (1.57 Å, Rwork = 15.6%, Rfree = 17.1%, residues 230 to 489) (Table 2). RESULTS 4 14 CD domains structure_element The CD domains of the truncated and full-length proteins superimpose with a 0.4-Å RMSD of the Cα backbone, with no differences in the position of any of the glycan-binding residues (see Fig. S7A in the supplemental material). RESULTS 22 31 truncated protein_state The CD domains of the truncated and full-length proteins superimpose with a 0.4-Å RMSD of the Cα backbone, with no differences in the position of any of the glycan-binding residues (see Fig. S7A in the supplemental material). RESULTS 36 47 full-length protein_state The CD domains of the truncated and full-length proteins superimpose with a 0.4-Å RMSD of the Cα backbone, with no differences in the position of any of the glycan-binding residues (see Fig. S7A in the supplemental material). RESULTS 57 68 superimpose experimental_method The CD domains of the truncated and full-length proteins superimpose with a 0.4-Å RMSD of the Cα backbone, with no differences in the position of any of the glycan-binding residues (see Fig. S7A in the supplemental material). RESULTS 82 86 RMSD evidence The CD domains of the truncated and full-length proteins superimpose with a 0.4-Å RMSD of the Cα backbone, with no differences in the position of any of the glycan-binding residues (see Fig. S7A in the supplemental material). RESULTS 157 180 glycan-binding residues site The CD domains of the truncated and full-length proteins superimpose with a 0.4-Å RMSD of the Cα backbone, with no differences in the position of any of the glycan-binding residues (see Fig. S7A in the supplemental material). RESULTS 6 13 density evidence While density is observed for XyGO2, the ligand could not be unambiguously modeled into this density to achieve a reasonable fit between the X-ray data and the known stereochemistry of the sugar (see Fig. S7B and C). RESULTS 30 35 XyGO2 chemical While density is observed for XyGO2, the ligand could not be unambiguously modeled into this density to achieve a reasonable fit between the X-ray data and the known stereochemistry of the sugar (see Fig. S7B and C). RESULTS 93 100 density evidence While density is observed for XyGO2, the ligand could not be unambiguously modeled into this density to achieve a reasonable fit between the X-ray data and the known stereochemistry of the sugar (see Fig. S7B and C). RESULTS 141 151 X-ray data evidence While density is observed for XyGO2, the ligand could not be unambiguously modeled into this density to achieve a reasonable fit between the X-ray data and the known stereochemistry of the sugar (see Fig. S7B and C). RESULTS 48 66 crystal structures evidence While this may occur for a number of reasons in crystal structures, it is likely that the poor ligand density even at higher resolution is due to movement or multiple orientations of the sugar averaged throughout the lattice. RESULTS 187 192 sugar chemical While this may occur for a number of reasons in crystal structures, it is likely that the poor ligand density even at higher resolution is due to movement or multiple orientations of the sugar averaged throughout the lattice. RESULTS 0 6 SGBP-A protein SGBP-A and SGBP-B have distinct, coordinated functions in vivo. RESULTS 11 17 SGBP-B protein SGBP-A and SGBP-B have distinct, coordinated functions in vivo. RESULTS 22 28 glycan chemical The similarity of the glycan specificity of SGBP-A and SGBP-B presents an intriguing conundrum regarding their individual roles in XyG utilization by B. ovatus. RESULTS 44 50 SGBP-A protein The similarity of the glycan specificity of SGBP-A and SGBP-B presents an intriguing conundrum regarding their individual roles in XyG utilization by B. ovatus. RESULTS 55 61 SGBP-B protein The similarity of the glycan specificity of SGBP-A and SGBP-B presents an intriguing conundrum regarding their individual roles in XyG utilization by B. ovatus. RESULTS 131 134 XyG chemical The similarity of the glycan specificity of SGBP-A and SGBP-B presents an intriguing conundrum regarding their individual roles in XyG utilization by B. ovatus. RESULTS 150 159 B. ovatus species The similarity of the glycan specificity of SGBP-A and SGBP-B presents an intriguing conundrum regarding their individual roles in XyG utilization by B. ovatus. RESULTS 32 38 SGBP-A protein To disentangle the functions of SGBP-A and SGBP-B in XyG recognition and uptake, we created individual in-frame deletion and complementation mutant strains of B. ovatus. RESULTS 43 49 SGBP-B protein To disentangle the functions of SGBP-A and SGBP-B in XyG recognition and uptake, we created individual in-frame deletion and complementation mutant strains of B. ovatus. RESULTS 53 56 XyG chemical To disentangle the functions of SGBP-A and SGBP-B in XyG recognition and uptake, we created individual in-frame deletion and complementation mutant strains of B. ovatus. RESULTS 103 147 in-frame deletion and complementation mutant experimental_method To disentangle the functions of SGBP-A and SGBP-B in XyG recognition and uptake, we created individual in-frame deletion and complementation mutant strains of B. ovatus. RESULTS 159 168 B. ovatus species To disentangle the functions of SGBP-A and SGBP-B in XyG recognition and uptake, we created individual in-frame deletion and complementation mutant strains of B. ovatus. RESULTS 9 27 growth experiments experimental_method In these growth experiments, overnight cultures of strains grown on minimal medium plus glucose were back-diluted 1:100-fold into minimal medium containing 5 mg/ml of the reported carbohydrate. RESULTS 88 95 glucose chemical In these growth experiments, overnight cultures of strains grown on minimal medium plus glucose were back-diluted 1:100-fold into minimal medium containing 5 mg/ml of the reported carbohydrate. RESULTS 180 192 carbohydrate chemical In these growth experiments, overnight cultures of strains grown on minimal medium plus glucose were back-diluted 1:100-fold into minimal medium containing 5 mg/ml of the reported carbohydrate. RESULTS 10 17 glucose chemical Growth on glucose displayed the shortest lag time for each strain, and so lag times were normalized for each carbohydrate by subtracting the lag time of that strain in glucose (Fig. 6; see Fig. S8 in the supplemental material). RESULTS 41 49 lag time evidence Growth on glucose displayed the shortest lag time for each strain, and so lag times were normalized for each carbohydrate by subtracting the lag time of that strain in glucose (Fig. 6; see Fig. S8 in the supplemental material). RESULTS 74 83 lag times evidence Growth on glucose displayed the shortest lag time for each strain, and so lag times were normalized for each carbohydrate by subtracting the lag time of that strain in glucose (Fig. 6; see Fig. S8 in the supplemental material). RESULTS 109 121 carbohydrate chemical Growth on glucose displayed the shortest lag time for each strain, and so lag times were normalized for each carbohydrate by subtracting the lag time of that strain in glucose (Fig. 6; see Fig. S8 in the supplemental material). RESULTS 141 149 lag time evidence Growth on glucose displayed the shortest lag time for each strain, and so lag times were normalized for each carbohydrate by subtracting the lag time of that strain in glucose (Fig. 6; see Fig. S8 in the supplemental material). RESULTS 168 175 glucose chemical Growth on glucose displayed the shortest lag time for each strain, and so lag times were normalized for each carbohydrate by subtracting the lag time of that strain in glucose (Fig. 6; see Fig. S8 in the supplemental material). RESULTS 29 34 XyGUL gene A strain in which the entire XyGUL is deleted displays a lag of 24.5 h during growth on glucose compared to the isogenic parental wild-type (WT) Δtdk strain, for which exponential growth lags for 19.8 h (see Fig. S8D). RESULTS 38 45 deleted experimental_method A strain in which the entire XyGUL is deleted displays a lag of 24.5 h during growth on glucose compared to the isogenic parental wild-type (WT) Δtdk strain, for which exponential growth lags for 19.8 h (see Fig. S8D). RESULTS 57 60 lag evidence A strain in which the entire XyGUL is deleted displays a lag of 24.5 h during growth on glucose compared to the isogenic parental wild-type (WT) Δtdk strain, for which exponential growth lags for 19.8 h (see Fig. S8D). RESULTS 88 95 glucose chemical A strain in which the entire XyGUL is deleted displays a lag of 24.5 h during growth on glucose compared to the isogenic parental wild-type (WT) Δtdk strain, for which exponential growth lags for 19.8 h (see Fig. S8D). RESULTS 130 139 wild-type protein_state A strain in which the entire XyGUL is deleted displays a lag of 24.5 h during growth on glucose compared to the isogenic parental wild-type (WT) Δtdk strain, for which exponential growth lags for 19.8 h (see Fig. S8D). RESULTS 141 143 WT protein_state A strain in which the entire XyGUL is deleted displays a lag of 24.5 h during growth on glucose compared to the isogenic parental wild-type (WT) Δtdk strain, for which exponential growth lags for 19.8 h (see Fig. S8D). RESULTS 145 149 Δtdk mutant A strain in which the entire XyGUL is deleted displays a lag of 24.5 h during growth on glucose compared to the isogenic parental wild-type (WT) Δtdk strain, for which exponential growth lags for 19.8 h (see Fig. S8D). RESULTS 187 191 lags evidence A strain in which the entire XyGUL is deleted displays a lag of 24.5 h during growth on glucose compared to the isogenic parental wild-type (WT) Δtdk strain, for which exponential growth lags for 19.8 h (see Fig. S8D). RESULTS 151 158 glucose chemical It is unknown whether this is because cultures were not normalized by the starting optical density (OD) or viable cells or reflects a minor defect for glucose utilization. RESULTS 91 98 glucose chemical The former seems more likely as the growth rates are nearly identical for these strains on glucose and xylose. RESULTS 103 109 xylose chemical The former seems more likely as the growth rates are nearly identical for these strains on glucose and xylose. RESULTS 4 10 ΔXyGUL mutant The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 15 17 WT protein_state The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 18 22 Δtdk mutant The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 50 59 lag times evidence The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 63 69 xylose chemical The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 183 191 lag time evidence The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 195 201 xylose chemical The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 211 213 WT protein_state The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 214 218 Δtdk mutant The ΔXyGUL and WT Δtdk strains display normalized lag times on xylose within experimental error, and curiously some of the mutant and complemented strains display a nominally shorter lag time on xylose than the WT Δtdk strain. RESULTS 0 15 Complementation experimental_method Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 23 30 ΔSGBP-A mutant Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 39 46 ΔSGBP-A mutant Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 48 54 SGBP-A protein Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 75 84 wild-type protein_state Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 94 104 xyloglucan chemical Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 109 114 XyGO1 chemical Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 187 189 WT protein_state Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 190 194 Δtdk mutant Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 205 210 XyGO2 chemical Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 250 256 SGBP-B protein Complementation of the ΔSGBP-A strain (ΔSGBP-A::SGBP-A) restores growth to wild-type rates on xyloglucan and XyGO1, yet the calculated rate of the complemented strain is ~72% that of the WT Δtdk strain on XyGO2; similar results were obtained for the SGBP-B complemented strain despite the fact that the growth curves do not appear much different (see Fig. S8C and F). RESULTS 35 40 XyGO2 chemical The reason for this observation on XyGO2 is unclear, as the ΔSGBP-B mutant does not have a significantly different growth rate from the WT on XyGO2. RESULTS 60 67 ΔSGBP-B mutant The reason for this observation on XyGO2 is unclear, as the ΔSGBP-B mutant does not have a significantly different growth rate from the WT on XyGO2. RESULTS 68 74 mutant protein_state The reason for this observation on XyGO2 is unclear, as the ΔSGBP-B mutant does not have a significantly different growth rate from the WT on XyGO2. RESULTS 136 138 WT protein_state The reason for this observation on XyGO2 is unclear, as the ΔSGBP-B mutant does not have a significantly different growth rate from the WT on XyGO2. RESULTS 142 147 XyGO2 chemical The reason for this observation on XyGO2 is unclear, as the ΔSGBP-B mutant does not have a significantly different growth rate from the WT on XyGO2. RESULTS 17 22 XyGUL gene Growth of select XyGUL mutants on xyloglucan and oligosaccharides. FIG 34 44 xyloglucan chemical Growth of select XyGUL mutants on xyloglucan and oligosaccharides. FIG 49 65 oligosaccharides chemical Growth of select XyGUL mutants on xyloglucan and oligosaccharides. FIG 0 9 B. ovatus species B. ovatus mutants were created in a thymidine kinase deletion (Δtdk) mutant as described previously. FIG 36 61 thymidine kinase deletion mutant B. ovatus mutants were created in a thymidine kinase deletion (Δtdk) mutant as described previously. FIG 63 67 Δtdk mutant B. ovatus mutants were created in a thymidine kinase deletion (Δtdk) mutant as described previously. FIG 0 7 SGBP-A* mutant SGBP-A* denotes the Bacova_02651 (W82A W283A W306A) allele, and the GH9 gene is Bacova_02649. FIG 20 32 Bacova_02651 gene SGBP-A* denotes the Bacova_02651 (W82A W283A W306A) allele, and the GH9 gene is Bacova_02649. FIG 34 38 W82A mutant SGBP-A* denotes the Bacova_02651 (W82A W283A W306A) allele, and the GH9 gene is Bacova_02649. FIG 39 44 W283A mutant SGBP-A* denotes the Bacova_02651 (W82A W283A W306A) allele, and the GH9 gene is Bacova_02649. FIG 45 50 W306A mutant SGBP-A* denotes the Bacova_02651 (W82A W283A W306A) allele, and the GH9 gene is Bacova_02649. FIG 68 71 GH9 protein SGBP-A* denotes the Bacova_02651 (W82A W283A W306A) allele, and the GH9 gene is Bacova_02649. FIG 80 92 Bacova_02649 gene SGBP-A* denotes the Bacova_02651 (W82A W283A W306A) allele, and the GH9 gene is Bacova_02649. FIG 63 66 XyG chemical Growth was measured over time in minimal medium containing (A) XyG, (B) XyGO2, (C) XyGO1, (D) glucose, and (E) xylose. FIG 72 77 XyGO2 chemical Growth was measured over time in minimal medium containing (A) XyG, (B) XyGO2, (C) XyGO1, (D) glucose, and (E) xylose. FIG 83 88 XyGO1 chemical Growth was measured over time in minimal medium containing (A) XyG, (B) XyGO2, (C) XyGO1, (D) glucose, and (E) xylose. FIG 94 101 glucose chemical Growth was measured over time in minimal medium containing (A) XyG, (B) XyGO2, (C) XyGO1, (D) glucose, and (E) xylose. FIG 111 117 xylose chemical Growth was measured over time in minimal medium containing (A) XyG, (B) XyGO2, (C) XyGO1, (D) glucose, and (E) xylose. FIG 115 123 lag time evidence In panel F, the growth rate of each strain on the five carbon sources is displayed, and in panel G, the normalized lag time of each culture, relative to its growth on glucose, is displayed. FIG 167 174 glucose chemical In panel F, the growth rate of each strain on the five carbon sources is displayed, and in panel G, the normalized lag time of each culture, relative to its growth on glucose, is displayed. FIG 79 81 WT protein_state Solid bars indicate conditions that are not statistically significant from the WT Δtdk cultures grown on the indicated carbohydrate, while open bars indicate a P value of <0.005 compared to the WT Δtdk strain. FIG 82 86 Δtdk mutant Solid bars indicate conditions that are not statistically significant from the WT Δtdk cultures grown on the indicated carbohydrate, while open bars indicate a P value of <0.005 compared to the WT Δtdk strain. FIG 119 131 carbohydrate chemical Solid bars indicate conditions that are not statistically significant from the WT Δtdk cultures grown on the indicated carbohydrate, while open bars indicate a P value of <0.005 compared to the WT Δtdk strain. FIG 194 196 WT protein_state Solid bars indicate conditions that are not statistically significant from the WT Δtdk cultures grown on the indicated carbohydrate, while open bars indicate a P value of <0.005 compared to the WT Δtdk strain. FIG 197 201 Δtdk mutant Solid bars indicate conditions that are not statistically significant from the WT Δtdk cultures grown on the indicated carbohydrate, while open bars indicate a P value of <0.005 compared to the WT Δtdk strain. FIG 184 191 ΔSGBP-A mutant Conditions denoted by the same letter (b, c, or d) are not statistically significant from each other but are significantly different from the condition labeled “a.” Complementation of ΔSGBP-A and ΔSBGP-B was performed by allelic exchange of the wild-type genes back into the genome for expression via the native promoter: these growth curves, quantified rates and lag times are displayed in Fig. S8 in the supplemental material. FIG 196 203 ΔSBGP-B mutant Conditions denoted by the same letter (b, c, or d) are not statistically significant from each other but are significantly different from the condition labeled “a.” Complementation of ΔSGBP-A and ΔSBGP-B was performed by allelic exchange of the wild-type genes back into the genome for expression via the native promoter: these growth curves, quantified rates and lag times are displayed in Fig. S8 in the supplemental material. FIG 245 254 wild-type protein_state Conditions denoted by the same letter (b, c, or d) are not statistically significant from each other but are significantly different from the condition labeled “a.” Complementation of ΔSGBP-A and ΔSBGP-B was performed by allelic exchange of the wild-type genes back into the genome for expression via the native promoter: these growth curves, quantified rates and lag times are displayed in Fig. S8 in the supplemental material. FIG 364 373 lag times evidence Conditions denoted by the same letter (b, c, or d) are not statistically significant from each other but are significantly different from the condition labeled “a.” Complementation of ΔSGBP-A and ΔSBGP-B was performed by allelic exchange of the wild-type genes back into the genome for expression via the native promoter: these growth curves, quantified rates and lag times are displayed in Fig. S8 in the supplemental material. FIG 4 11 ΔSGBP-A mutant The ΔSGBP-A (ΔBacova_02651) strain (cf. RESULTS 13 26 ΔBacova_02651 mutant The ΔSGBP-A (ΔBacova_02651) strain (cf. RESULTS 47 50 XyG chemical Fig. 1B) was completely incapable of growth on XyG, XyGO1, and XyGO2, indicating that SGBP-A is essential for XyG utilization (Fig. 6). RESULTS 52 57 XyGO1 chemical Fig. 1B) was completely incapable of growth on XyG, XyGO1, and XyGO2, indicating that SGBP-A is essential for XyG utilization (Fig. 6). RESULTS 63 68 XyGO2 chemical Fig. 1B) was completely incapable of growth on XyG, XyGO1, and XyGO2, indicating that SGBP-A is essential for XyG utilization (Fig. 6). RESULTS 86 92 SGBP-A protein Fig. 1B) was completely incapable of growth on XyG, XyGO1, and XyGO2, indicating that SGBP-A is essential for XyG utilization (Fig. 6). RESULTS 110 113 XyG chemical Fig. 1B) was completely incapable of growth on XyG, XyGO1, and XyGO2, indicating that SGBP-A is essential for XyG utilization (Fig. 6). RESULTS 56 59 Sus complex_assembly This result mirrors our previous data for the canonical Sus of B. thetaiotaomicron, which revealed that a homologous ΔsusD mutant is unable to grow on starch or malto-oligosaccharides, despite normal cell surface expression of all other PUL-encoded proteins. RESULTS 63 82 B. thetaiotaomicron species This result mirrors our previous data for the canonical Sus of B. thetaiotaomicron, which revealed that a homologous ΔsusD mutant is unable to grow on starch or malto-oligosaccharides, despite normal cell surface expression of all other PUL-encoded proteins. RESULTS 117 122 ΔsusD mutant This result mirrors our previous data for the canonical Sus of B. thetaiotaomicron, which revealed that a homologous ΔsusD mutant is unable to grow on starch or malto-oligosaccharides, despite normal cell surface expression of all other PUL-encoded proteins. RESULTS 123 129 mutant protein_state This result mirrors our previous data for the canonical Sus of B. thetaiotaomicron, which revealed that a homologous ΔsusD mutant is unable to grow on starch or malto-oligosaccharides, despite normal cell surface expression of all other PUL-encoded proteins. RESULTS 151 157 starch chemical This result mirrors our previous data for the canonical Sus of B. thetaiotaomicron, which revealed that a homologous ΔsusD mutant is unable to grow on starch or malto-oligosaccharides, despite normal cell surface expression of all other PUL-encoded proteins. RESULTS 161 183 malto-oligosaccharides chemical This result mirrors our previous data for the canonical Sus of B. thetaiotaomicron, which revealed that a homologous ΔsusD mutant is unable to grow on starch or malto-oligosaccharides, despite normal cell surface expression of all other PUL-encoded proteins. RESULTS 237 240 PUL gene This result mirrors our previous data for the canonical Sus of B. thetaiotaomicron, which revealed that a homologous ΔsusD mutant is unable to grow on starch or malto-oligosaccharides, despite normal cell surface expression of all other PUL-encoded proteins. RESULTS 98 102 SusD protein More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 104 119 complementation experimental_method More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 123 128 ΔsusD mutant More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 134 139 SusD* mutant More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 143 170 triple site-directed mutant protein_state More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 172 176 W96A mutant More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 177 182 W320A mutant More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 183 188 Y296A mutant More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 195 217 ablates glycan binding protein_state More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 228 247 B. thetaiotaomicron species More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 258 280 malto-oligosaccharides chemical More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 285 291 starch chemical More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 297 300 sus gene More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 329 336 maltose chemical More recently, we demonstrated that this phenotype is due to the loss of the physical presence of SusD; complementation of ΔsusD with SusD*, a triple site-directed mutant (W96A W320A Y296A) that ablates glycan binding, restores B. thetaiotaomicron growth on malto-oligosaccharides and starch when sus transcription is induced by maltose addition. RESULTS 27 33 SGBP-A protein Similarly, the function of SGBP-A extends beyond glycan binding. RESULTS 49 55 glycan chemical Similarly, the function of SGBP-A extends beyond glycan binding. RESULTS 0 15 Complementation experimental_method Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 19 26 ΔSGBP-A mutant Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 36 43 SGBP-A* mutant Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 45 49 W82A mutant Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 50 55 W283A mutant Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 56 61 W306A mutant Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 83 91 not bind protein_state Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 92 95 XyG chemical Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 116 119 XyG chemical Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 124 129 XyGOs chemical Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 139 146 ΔSGBP-A mutant Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 148 155 SGBP-A* mutant Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 202 204 WT protein_state Complementation of ΔSGBP-A with the SGBP-A* (W82A W283A W306A) variant, which does not bind XyG, supports growth on XyG and XyGOs (Fig. 6; ΔSGBP-A::SGBP-A*), with growth rates that are ~70% that of the WT. RESULTS 38 50 carbohydrate chemical In previous studies, we observed that carbohydrate binding by SusD enhanced the sensitivity of the cells to limiting concentrations of malto-oligosaccharides by several orders of magnitude, such that the addition of 0.5 g/liter maltose was required to restore growth of the ΔsusD::SusD* strain on starch, which nonetheless occurred following an extended lag phase. RESULTS 62 66 SusD protein In previous studies, we observed that carbohydrate binding by SusD enhanced the sensitivity of the cells to limiting concentrations of malto-oligosaccharides by several orders of magnitude, such that the addition of 0.5 g/liter maltose was required to restore growth of the ΔsusD::SusD* strain on starch, which nonetheless occurred following an extended lag phase. RESULTS 228 235 maltose chemical In previous studies, we observed that carbohydrate binding by SusD enhanced the sensitivity of the cells to limiting concentrations of malto-oligosaccharides by several orders of magnitude, such that the addition of 0.5 g/liter maltose was required to restore growth of the ΔsusD::SusD* strain on starch, which nonetheless occurred following an extended lag phase. RESULTS 274 279 ΔsusD mutant In previous studies, we observed that carbohydrate binding by SusD enhanced the sensitivity of the cells to limiting concentrations of malto-oligosaccharides by several orders of magnitude, such that the addition of 0.5 g/liter maltose was required to restore growth of the ΔsusD::SusD* strain on starch, which nonetheless occurred following an extended lag phase. RESULTS 281 286 SusD* mutant In previous studies, we observed that carbohydrate binding by SusD enhanced the sensitivity of the cells to limiting concentrations of malto-oligosaccharides by several orders of magnitude, such that the addition of 0.5 g/liter maltose was required to restore growth of the ΔsusD::SusD* strain on starch, which nonetheless occurred following an extended lag phase. RESULTS 297 303 starch chemical In previous studies, we observed that carbohydrate binding by SusD enhanced the sensitivity of the cells to limiting concentrations of malto-oligosaccharides by several orders of magnitude, such that the addition of 0.5 g/liter maltose was required to restore growth of the ΔsusD::SusD* strain on starch, which nonetheless occurred following an extended lag phase. RESULTS 354 363 lag phase evidence In previous studies, we observed that carbohydrate binding by SusD enhanced the sensitivity of the cells to limiting concentrations of malto-oligosaccharides by several orders of magnitude, such that the addition of 0.5 g/liter maltose was required to restore growth of the ΔsusD::SusD* strain on starch, which nonetheless occurred following an extended lag phase. RESULTS 17 24 ΔSGBP-A mutant In contrast, the ΔSGBP-A::SGBP-A* strain does not display an extended lag time on any of the xyloglucan substrates compared to the WT (Fig. 6). RESULTS 26 33 SGBP-A* mutant In contrast, the ΔSGBP-A::SGBP-A* strain does not display an extended lag time on any of the xyloglucan substrates compared to the WT (Fig. 6). RESULTS 70 78 lag time evidence In contrast, the ΔSGBP-A::SGBP-A* strain does not display an extended lag time on any of the xyloglucan substrates compared to the WT (Fig. 6). RESULTS 93 103 xyloglucan chemical In contrast, the ΔSGBP-A::SGBP-A* strain does not display an extended lag time on any of the xyloglucan substrates compared to the WT (Fig. 6). RESULTS 131 133 WT protein_state In contrast, the ΔSGBP-A::SGBP-A* strain does not display an extended lag time on any of the xyloglucan substrates compared to the WT (Fig. 6). RESULTS 13 19 glycan chemical The specific glycan signal that upregulates BoXyGUL is currently unknown. RESULTS 44 51 BoXyGUL gene The specific glycan signal that upregulates BoXyGUL is currently unknown. RESULTS 68 74 glycan chemical From our present data, we cannot eliminate the possibility that the glycan binding by SGBP-A enhances transcriptional activation of the XyGUL. RESULTS 86 92 SGBP-A protein From our present data, we cannot eliminate the possibility that the glycan binding by SGBP-A enhances transcriptional activation of the XyGUL. RESULTS 136 141 XyGUL gene From our present data, we cannot eliminate the possibility that the glycan binding by SGBP-A enhances transcriptional activation of the XyGUL. RESULTS 49 55 SGBP-A protein However, the modest rate defect displayed by the SGBP-A::SGBP-A* strain suggests that recognition of XyG and product import is somewhat less efficient in these cells. RESULTS 57 64 SGBP-A* mutant However, the modest rate defect displayed by the SGBP-A::SGBP-A* strain suggests that recognition of XyG and product import is somewhat less efficient in these cells. RESULTS 101 104 XyG chemical However, the modest rate defect displayed by the SGBP-A::SGBP-A* strain suggests that recognition of XyG and product import is somewhat less efficient in these cells. RESULTS 18 25 ΔSGBP-B mutant Intriguingly, the ΔSGBP-B strain (ΔBacova_02650) (cf. RESULTS 34 47 ΔBacova_02650 mutant Intriguingly, the ΔSGBP-B strain (ΔBacova_02650) (cf. RESULTS 49 52 XyG chemical Fig. 1B) exhibited a minor growth defect on both XyG and XyGO2, with rates 84.6% and 93.9% that of the WT Δtdk strain. RESULTS 57 62 XyGO2 chemical Fig. 1B) exhibited a minor growth defect on both XyG and XyGO2, with rates 84.6% and 93.9% that of the WT Δtdk strain. RESULTS 103 105 WT protein_state Fig. 1B) exhibited a minor growth defect on both XyG and XyGO2, with rates 84.6% and 93.9% that of the WT Δtdk strain. RESULTS 106 110 Δtdk mutant Fig. 1B) exhibited a minor growth defect on both XyG and XyGO2, with rates 84.6% and 93.9% that of the WT Δtdk strain. RESULTS 23 30 ΔSGBP-B mutant However, growth of the ΔSGBP-B strain on XyGO1 was 54.2% the rate of the parental strain, despite the fact that SGBP-B binds this substrate ca. RESULTS 41 46 XyGO1 chemical However, growth of the ΔSGBP-B strain on XyGO1 was 54.2% the rate of the parental strain, despite the fact that SGBP-B binds this substrate ca. RESULTS 112 118 SGBP-B protein However, growth of the ΔSGBP-B strain on XyGO1 was 54.2% the rate of the parental strain, despite the fact that SGBP-B binds this substrate ca. RESULTS 25 30 XyGO2 chemical 10-fold more weakly than XyGO2 and XyG (Fig. 6; Table 1). RESULTS 35 38 XyG chemical 10-fold more weakly than XyGO2 and XyG (Fig. 6; Table 1). RESULTS 31 37 SGBP-A protein As such, the data suggest that SGBP-A can compensate for the loss of function of SGBP-B on longer oligo- and polysaccharides, while SGBP-B may adapt the cell to recognize smaller oligosaccharides efficiently. RESULTS 81 87 SGBP-B protein As such, the data suggest that SGBP-A can compensate for the loss of function of SGBP-B on longer oligo- and polysaccharides, while SGBP-B may adapt the cell to recognize smaller oligosaccharides efficiently. RESULTS 98 124 oligo- and polysaccharides chemical As such, the data suggest that SGBP-A can compensate for the loss of function of SGBP-B on longer oligo- and polysaccharides, while SGBP-B may adapt the cell to recognize smaller oligosaccharides efficiently. RESULTS 132 138 SGBP-B protein As such, the data suggest that SGBP-A can compensate for the loss of function of SGBP-B on longer oligo- and polysaccharides, while SGBP-B may adapt the cell to recognize smaller oligosaccharides efficiently. RESULTS 179 195 oligosaccharides chemical As such, the data suggest that SGBP-A can compensate for the loss of function of SGBP-B on longer oligo- and polysaccharides, while SGBP-B may adapt the cell to recognize smaller oligosaccharides efficiently. RESULTS 10 23 double mutant protein_state Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 41 49 crippled protein_state Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 50 56 SGBP-A protein Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 63 74 deletion of experimental_method Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 75 81 SGBP-B protein Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 83 90 ΔSGBP-A mutant Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 92 99 SGBP-A* mutant Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 100 107 ΔSGBP-B mutant Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 131 139 lag time evidence Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 148 151 XyG chemical Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 156 161 XyGO2 chemical Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 174 179 XyGO1 chemical Indeed, a double mutant, consisting of a crippled SGBP-A and a deletion of SGBP-B (ΔSGBP-A::SGBP-A*/ΔSGBP-B), exhibits an extended lag time on both XyG and XyGO2, as well as XyGO1. RESULTS 39 45 SGBP-A protein Taken together, the data indicate that SGBP-A and SGBP-B functionally complement each other in the capture of XyG polysaccharide, while SGBP-B may allow B. ovatus to scavenge smaller XyGOs liberated by other gut commensals. RESULTS 50 56 SGBP-B protein Taken together, the data indicate that SGBP-A and SGBP-B functionally complement each other in the capture of XyG polysaccharide, while SGBP-B may allow B. ovatus to scavenge smaller XyGOs liberated by other gut commensals. RESULTS 110 113 XyG chemical Taken together, the data indicate that SGBP-A and SGBP-B functionally complement each other in the capture of XyG polysaccharide, while SGBP-B may allow B. ovatus to scavenge smaller XyGOs liberated by other gut commensals. RESULTS 114 128 polysaccharide chemical Taken together, the data indicate that SGBP-A and SGBP-B functionally complement each other in the capture of XyG polysaccharide, while SGBP-B may allow B. ovatus to scavenge smaller XyGOs liberated by other gut commensals. RESULTS 136 142 SGBP-B protein Taken together, the data indicate that SGBP-A and SGBP-B functionally complement each other in the capture of XyG polysaccharide, while SGBP-B may allow B. ovatus to scavenge smaller XyGOs liberated by other gut commensals. RESULTS 153 162 B. ovatus species Taken together, the data indicate that SGBP-A and SGBP-B functionally complement each other in the capture of XyG polysaccharide, while SGBP-B may allow B. ovatus to scavenge smaller XyGOs liberated by other gut commensals. RESULTS 183 188 XyGOs chemical Taken together, the data indicate that SGBP-A and SGBP-B functionally complement each other in the capture of XyG polysaccharide, while SGBP-B may allow B. ovatus to scavenge smaller XyGOs liberated by other gut commensals. RESULTS 24 30 SGBP-B protein This additional role of SGBP-B is especially notable in the context of studies on BtSusE and BtSusF (positioned similarly in the archetypal Sus locus) (Fig. 1B), for which growth defects on starch or malto-oligosaccharides have never been observed. RESULTS 82 88 BtSusE protein This additional role of SGBP-B is especially notable in the context of studies on BtSusE and BtSusF (positioned similarly in the archetypal Sus locus) (Fig. 1B), for which growth defects on starch or malto-oligosaccharides have never been observed. RESULTS 93 99 BtSusF protein This additional role of SGBP-B is especially notable in the context of studies on BtSusE and BtSusF (positioned similarly in the archetypal Sus locus) (Fig. 1B), for which growth defects on starch or malto-oligosaccharides have never been observed. RESULTS 140 149 Sus locus gene This additional role of SGBP-B is especially notable in the context of studies on BtSusE and BtSusF (positioned similarly in the archetypal Sus locus) (Fig. 1B), for which growth defects on starch or malto-oligosaccharides have never been observed. RESULTS 190 196 starch chemical This additional role of SGBP-B is especially notable in the context of studies on BtSusE and BtSusF (positioned similarly in the archetypal Sus locus) (Fig. 1B), for which growth defects on starch or malto-oligosaccharides have never been observed. RESULTS 200 222 malto-oligosaccharides chemical This additional role of SGBP-B is especially notable in the context of studies on BtSusE and BtSusF (positioned similarly in the archetypal Sus locus) (Fig. 1B), for which growth defects on starch or malto-oligosaccharides have never been observed. RESULTS 7 13 SGBP-A protein Beyond SGBP-A and SGBP-B, we speculated that the catalytically feeble endo-xyloglucanase GH9, which is expendable for growth in the presence of GH5, might also play a role in glycan binding to the cell surface. RESULTS 18 24 SGBP-B protein Beyond SGBP-A and SGBP-B, we speculated that the catalytically feeble endo-xyloglucanase GH9, which is expendable for growth in the presence of GH5, might also play a role in glycan binding to the cell surface. RESULTS 49 69 catalytically feeble protein_state Beyond SGBP-A and SGBP-B, we speculated that the catalytically feeble endo-xyloglucanase GH9, which is expendable for growth in the presence of GH5, might also play a role in glycan binding to the cell surface. RESULTS 70 88 endo-xyloglucanase protein_type Beyond SGBP-A and SGBP-B, we speculated that the catalytically feeble endo-xyloglucanase GH9, which is expendable for growth in the presence of GH5, might also play a role in glycan binding to the cell surface. RESULTS 89 92 GH9 protein Beyond SGBP-A and SGBP-B, we speculated that the catalytically feeble endo-xyloglucanase GH9, which is expendable for growth in the presence of GH5, might also play a role in glycan binding to the cell surface. RESULTS 144 147 GH5 protein Beyond SGBP-A and SGBP-B, we speculated that the catalytically feeble endo-xyloglucanase GH9, which is expendable for growth in the presence of GH5, might also play a role in glycan binding to the cell surface. RESULTS 175 181 glycan chemical Beyond SGBP-A and SGBP-B, we speculated that the catalytically feeble endo-xyloglucanase GH9, which is expendable for growth in the presence of GH5, might also play a role in glycan binding to the cell surface. RESULTS 9 48 combined deletion of the genes encoding experimental_method However, combined deletion of the genes encoding GH9 (encoded by Bacova_02649) and SGBP-B does not exacerbate the growth defect on XyGO1 (Fig. 6; ΔSGBP-B/ΔGH9). RESULTS 49 52 GH9 protein However, combined deletion of the genes encoding GH9 (encoded by Bacova_02649) and SGBP-B does not exacerbate the growth defect on XyGO1 (Fig. 6; ΔSGBP-B/ΔGH9). RESULTS 65 77 Bacova_02649 gene However, combined deletion of the genes encoding GH9 (encoded by Bacova_02649) and SGBP-B does not exacerbate the growth defect on XyGO1 (Fig. 6; ΔSGBP-B/ΔGH9). RESULTS 83 89 SGBP-B protein However, combined deletion of the genes encoding GH9 (encoded by Bacova_02649) and SGBP-B does not exacerbate the growth defect on XyGO1 (Fig. 6; ΔSGBP-B/ΔGH9). RESULTS 131 136 XyGO1 chemical However, combined deletion of the genes encoding GH9 (encoded by Bacova_02649) and SGBP-B does not exacerbate the growth defect on XyGO1 (Fig. 6; ΔSGBP-B/ΔGH9). RESULTS 146 153 ΔSGBP-B mutant However, combined deletion of the genes encoding GH9 (encoded by Bacova_02649) and SGBP-B does not exacerbate the growth defect on XyGO1 (Fig. 6; ΔSGBP-B/ΔGH9). RESULTS 154 158 ΔGH9 mutant However, combined deletion of the genes encoding GH9 (encoded by Bacova_02649) and SGBP-B does not exacerbate the growth defect on XyGO1 (Fig. 6; ΔSGBP-B/ΔGH9). RESULTS 17 23 SGBP-B protein The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 43 50 SGBP-A* mutant The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 66 73 ΔSGBP-A mutant The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 75 82 SGBP-A* mutant The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 84 91 ΔSGBP-B mutant The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 92 98 mutant protein_state The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 120 123 lag evidence The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 141 144 XyG chemical The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 149 175 xylogluco-oligosaccharides chemical The necessity of SGBP-B is elevated in the SGBP-A* strain, as the ΔSGBP-A::SGBP-A*/ ΔSGBP-B mutant displays an extended lag during growth on XyG and xylogluco-oligosaccharides, while growth rate differences are more subtle. RESULTS 28 31 lag evidence The precise reason for this lag is unclear, but recapitulating our findings on the role of SusD in malto-oligosaccharide sensing in B. thetaiotaomicron, this extended lag may be due to inefficient import and thus sensing of xyloglucan in the environment in the absence of glycan binding by essential SGBPs. RESULTS 91 95 SusD protein The precise reason for this lag is unclear, but recapitulating our findings on the role of SusD in malto-oligosaccharide sensing in B. thetaiotaomicron, this extended lag may be due to inefficient import and thus sensing of xyloglucan in the environment in the absence of glycan binding by essential SGBPs. RESULTS 99 120 malto-oligosaccharide chemical The precise reason for this lag is unclear, but recapitulating our findings on the role of SusD in malto-oligosaccharide sensing in B. thetaiotaomicron, this extended lag may be due to inefficient import and thus sensing of xyloglucan in the environment in the absence of glycan binding by essential SGBPs. RESULTS 132 151 B. thetaiotaomicron species The precise reason for this lag is unclear, but recapitulating our findings on the role of SusD in malto-oligosaccharide sensing in B. thetaiotaomicron, this extended lag may be due to inefficient import and thus sensing of xyloglucan in the environment in the absence of glycan binding by essential SGBPs. RESULTS 167 170 lag evidence The precise reason for this lag is unclear, but recapitulating our findings on the role of SusD in malto-oligosaccharide sensing in B. thetaiotaomicron, this extended lag may be due to inefficient import and thus sensing of xyloglucan in the environment in the absence of glycan binding by essential SGBPs. RESULTS 224 234 xyloglucan chemical The precise reason for this lag is unclear, but recapitulating our findings on the role of SusD in malto-oligosaccharide sensing in B. thetaiotaomicron, this extended lag may be due to inefficient import and thus sensing of xyloglucan in the environment in the absence of glycan binding by essential SGBPs. RESULTS 272 278 glycan chemical The precise reason for this lag is unclear, but recapitulating our findings on the role of SusD in malto-oligosaccharide sensing in B. thetaiotaomicron, this extended lag may be due to inefficient import and thus sensing of xyloglucan in the environment in the absence of glycan binding by essential SGBPs. RESULTS 300 305 SGBPs protein_type The precise reason for this lag is unclear, but recapitulating our findings on the role of SusD in malto-oligosaccharide sensing in B. thetaiotaomicron, this extended lag may be due to inefficient import and thus sensing of xyloglucan in the environment in the absence of glycan binding by essential SGBPs. RESULTS 36 45 B. ovatus species Our previous work demonstrates that B. ovatus cells grown in minimal medium plus glucose express low levels of the XyGUL transcript. RESULTS 81 88 glucose chemical Our previous work demonstrates that B. ovatus cells grown in minimal medium plus glucose express low levels of the XyGUL transcript. RESULTS 115 120 XyGUL gene Our previous work demonstrates that B. ovatus cells grown in minimal medium plus glucose express low levels of the XyGUL transcript. RESULTS 74 81 glucose chemical Thus, in our experiments, we presume that each strain, initially grown in glucose, expresses low levels of the XyGUL transcript and thus low levels of the XyGUL-encoded surface proteins, including the vanguard GH5. RESULTS 111 116 XyGUL gene Thus, in our experiments, we presume that each strain, initially grown in glucose, expresses low levels of the XyGUL transcript and thus low levels of the XyGUL-encoded surface proteins, including the vanguard GH5. RESULTS 155 160 XyGUL gene Thus, in our experiments, we presume that each strain, initially grown in glucose, expresses low levels of the XyGUL transcript and thus low levels of the XyGUL-encoded surface proteins, including the vanguard GH5. RESULTS 210 213 GH5 protein Thus, in our experiments, we presume that each strain, initially grown in glucose, expresses low levels of the XyGUL transcript and thus low levels of the XyGUL-encoded surface proteins, including the vanguard GH5. RESULTS 19 25 glycan chemical Presumably without glycan binding by the SGBPs, the GH5 protein cannot efficiently process xyloglucan, and/or the lack of SGBP function prevents efficient capture and import of the processed oligosaccharides. RESULTS 41 46 SGBPs protein_type Presumably without glycan binding by the SGBPs, the GH5 protein cannot efficiently process xyloglucan, and/or the lack of SGBP function prevents efficient capture and import of the processed oligosaccharides. RESULTS 52 55 GH5 protein Presumably without glycan binding by the SGBPs, the GH5 protein cannot efficiently process xyloglucan, and/or the lack of SGBP function prevents efficient capture and import of the processed oligosaccharides. RESULTS 91 101 xyloglucan chemical Presumably without glycan binding by the SGBPs, the GH5 protein cannot efficiently process xyloglucan, and/or the lack of SGBP function prevents efficient capture and import of the processed oligosaccharides. RESULTS 122 126 SGBP protein_type Presumably without glycan binding by the SGBPs, the GH5 protein cannot efficiently process xyloglucan, and/or the lack of SGBP function prevents efficient capture and import of the processed oligosaccharides. RESULTS 191 207 oligosaccharides chemical Presumably without glycan binding by the SGBPs, the GH5 protein cannot efficiently process xyloglucan, and/or the lack of SGBP function prevents efficient capture and import of the processed oligosaccharides. RESULTS 54 60 glycan chemical It may then be that only after a sufficient amount of glycan is processed and imported by the cell is XyGUL upregulated and exponential growth on the glycan can begin. RESULTS 102 107 XyGUL gene It may then be that only after a sufficient amount of glycan is processed and imported by the cell is XyGUL upregulated and exponential growth on the glycan can begin. RESULTS 150 156 glycan chemical It may then be that only after a sufficient amount of glycan is processed and imported by the cell is XyGUL upregulated and exponential growth on the glycan can begin. RESULTS 68 74 SGBP-A protein We hypothesize that during exponential growth the essential role of SGBP-A extends beyond glycan recognition, perhaps due to a critical interaction with the TBDT. RESULTS 90 96 glycan chemical We hypothesize that during exponential growth the essential role of SGBP-A extends beyond glycan recognition, perhaps due to a critical interaction with the TBDT. RESULTS 157 161 TBDT protein_type We hypothesize that during exponential growth the essential role of SGBP-A extends beyond glycan recognition, perhaps due to a critical interaction with the TBDT. RESULTS 7 12 BtSus gene In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 14 18 SusD protein In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 27 31 TBDT protein_type In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 32 36 SusC protein In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 103 109 glycan chemical In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 150 155 ΔsusD mutant In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 156 162 mutant protein_state In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 178 184 starch chemical In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 192 197 ΔsusD mutant In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 199 204 SusD* mutant In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 238 263 transcriptional activator protein_type In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 271 281 sus operon gene In the BtSus, SusD and the TBDT SusC interact, and we speculate that this interaction is necessary for glycan uptake, as suggested by the fact that a ΔsusD mutant cannot grow on starch, but a ΔsusD::SusD* strain regains this ability if a transcriptional activator of the sus operon is supplied. RESULTS 77 83 SGBP-A protein Likewise, such cognate interactions between homologous protein pairs such as SGBP-A and its TBDT may underlie our observation that a ΔSGBP-A mutant cannot grow on xyloglucan. RESULTS 92 96 TBDT protein_type Likewise, such cognate interactions between homologous protein pairs such as SGBP-A and its TBDT may underlie our observation that a ΔSGBP-A mutant cannot grow on xyloglucan. RESULTS 133 140 ΔSGBP-A mutant Likewise, such cognate interactions between homologous protein pairs such as SGBP-A and its TBDT may underlie our observation that a ΔSGBP-A mutant cannot grow on xyloglucan. RESULTS 141 147 mutant protein_state Likewise, such cognate interactions between homologous protein pairs such as SGBP-A and its TBDT may underlie our observation that a ΔSGBP-A mutant cannot grow on xyloglucan. RESULTS 163 173 xyloglucan chemical Likewise, such cognate interactions between homologous protein pairs such as SGBP-A and its TBDT may underlie our observation that a ΔSGBP-A mutant cannot grow on xyloglucan. RESULTS 20 23 Sus complex_assembly However, unlike the Sus, in which elimination of SusE and SusF does not affect growth on starch, SGBP-B appears to have a dedicated role in growth on small xylogluco-oligosaccharides. RESULTS 34 48 elimination of experimental_method However, unlike the Sus, in which elimination of SusE and SusF does not affect growth on starch, SGBP-B appears to have a dedicated role in growth on small xylogluco-oligosaccharides. RESULTS 49 53 SusE protein However, unlike the Sus, in which elimination of SusE and SusF does not affect growth on starch, SGBP-B appears to have a dedicated role in growth on small xylogluco-oligosaccharides. RESULTS 58 62 SusF protein However, unlike the Sus, in which elimination of SusE and SusF does not affect growth on starch, SGBP-B appears to have a dedicated role in growth on small xylogluco-oligosaccharides. RESULTS 89 95 starch chemical However, unlike the Sus, in which elimination of SusE and SusF does not affect growth on starch, SGBP-B appears to have a dedicated role in growth on small xylogluco-oligosaccharides. RESULTS 97 103 SGBP-B protein However, unlike the Sus, in which elimination of SusE and SusF does not affect growth on starch, SGBP-B appears to have a dedicated role in growth on small xylogluco-oligosaccharides. RESULTS 156 182 xylogluco-oligosaccharides chemical However, unlike the Sus, in which elimination of SusE and SusF does not affect growth on starch, SGBP-B appears to have a dedicated role in growth on small xylogluco-oligosaccharides. RESULTS 27 41 microorganisms taxonomy_domain The ability of gut-adapted microorganisms to thrive in the gastrointestinal tract is critically dependent upon their ability to efficiently recognize, cleave, and import glycans. RESULTS 170 177 glycans chemical The ability of gut-adapted microorganisms to thrive in the gastrointestinal tract is critically dependent upon their ability to efficiently recognize, cleave, and import glycans. RESULTS 4 9 human species The human gut, in particular, is a densely packed ecosystem with hundreds of species, in which there is potential for both competition and synergy in the utilization of different substrates. RESULTS 32 45 Bacteroidetes taxonomy_domain Recent work has elucidated that Bacteroidetes cross-feed during growth on many glycans; the glycoside hydrolases expressed by one species liberate oligosaccharides for consumption by other members of the community. RESULTS 79 86 glycans chemical Recent work has elucidated that Bacteroidetes cross-feed during growth on many glycans; the glycoside hydrolases expressed by one species liberate oligosaccharides for consumption by other members of the community. RESULTS 92 112 glycoside hydrolases protein_type Recent work has elucidated that Bacteroidetes cross-feed during growth on many glycans; the glycoside hydrolases expressed by one species liberate oligosaccharides for consumption by other members of the community. RESULTS 147 163 oligosaccharides chemical Recent work has elucidated that Bacteroidetes cross-feed during growth on many glycans; the glycoside hydrolases expressed by one species liberate oligosaccharides for consumption by other members of the community. RESULTS 20 26 glycan chemical Thus, understanding glycan capture at the cell surface is fundamental to explaining, and eventually predicting, how the carbohydrate content of the diet shapes the gut community structure as well as its causative health effects. RESULTS 30 61 surface glycan binding proteins protein_type Here, we demonstrate that the surface glycan binding proteins encoded within the BoXyGUL play unique and essential roles in the acquisition of the ubiquitous and abundant vegetable polysaccharide xyloglucan. RESULTS 81 88 BoXyGUL gene Here, we demonstrate that the surface glycan binding proteins encoded within the BoXyGUL play unique and essential roles in the acquisition of the ubiquitous and abundant vegetable polysaccharide xyloglucan. RESULTS 171 180 vegetable taxonomy_domain Here, we demonstrate that the surface glycan binding proteins encoded within the BoXyGUL play unique and essential roles in the acquisition of the ubiquitous and abundant vegetable polysaccharide xyloglucan. RESULTS 181 195 polysaccharide chemical Here, we demonstrate that the surface glycan binding proteins encoded within the BoXyGUL play unique and essential roles in the acquisition of the ubiquitous and abundant vegetable polysaccharide xyloglucan. RESULTS 196 206 xyloglucan chemical Here, we demonstrate that the surface glycan binding proteins encoded within the BoXyGUL play unique and essential roles in the acquisition of the ubiquitous and abundant vegetable polysaccharide xyloglucan. RESULTS 71 76 SGBPs protein_type Yet, a number of questions remain regarding the molecular interplay of SGBPs with their cotranscribed cohort of glycoside hydrolases and TonB-dependent transporters. RESULTS 112 132 glycoside hydrolases protein_type Yet, a number of questions remain regarding the molecular interplay of SGBPs with their cotranscribed cohort of glycoside hydrolases and TonB-dependent transporters. RESULTS 137 164 TonB-dependent transporters protein_type Yet, a number of questions remain regarding the molecular interplay of SGBPs with their cotranscribed cohort of glycoside hydrolases and TonB-dependent transporters. RESULTS 38 44 glycan chemical A particularly understudied aspect of glycan utilization is the mechanism of import via TBDTs (SusC homologs) (Fig. 1), which are ubiquitous and defining components of all PUL. RESULTS 88 93 TBDTs protein_type A particularly understudied aspect of glycan utilization is the mechanism of import via TBDTs (SusC homologs) (Fig. 1), which are ubiquitous and defining components of all PUL. RESULTS 95 99 SusC protein A particularly understudied aspect of glycan utilization is the mechanism of import via TBDTs (SusC homologs) (Fig. 1), which are ubiquitous and defining components of all PUL. RESULTS 172 175 PUL gene A particularly understudied aspect of glycan utilization is the mechanism of import via TBDTs (SusC homologs) (Fig. 1), which are ubiquitous and defining components of all PUL. RESULTS 0 3 PUL gene PUL-encoded TBDTs in Bacteroidetes are larger than the well-characterized iron-targeting TBDTs from many Proteobacteria and are further distinguished as the only known glycan-importing TBDTs coexpressed with an SGBP. RESULTS 12 17 TBDTs protein_type PUL-encoded TBDTs in Bacteroidetes are larger than the well-characterized iron-targeting TBDTs from many Proteobacteria and are further distinguished as the only known glycan-importing TBDTs coexpressed with an SGBP. RESULTS 21 34 Bacteroidetes taxonomy_domain PUL-encoded TBDTs in Bacteroidetes are larger than the well-characterized iron-targeting TBDTs from many Proteobacteria and are further distinguished as the only known glycan-importing TBDTs coexpressed with an SGBP. RESULTS 74 94 iron-targeting TBDTs protein_type PUL-encoded TBDTs in Bacteroidetes are larger than the well-characterized iron-targeting TBDTs from many Proteobacteria and are further distinguished as the only known glycan-importing TBDTs coexpressed with an SGBP. RESULTS 105 119 Proteobacteria taxonomy_domain PUL-encoded TBDTs in Bacteroidetes are larger than the well-characterized iron-targeting TBDTs from many Proteobacteria and are further distinguished as the only known glycan-importing TBDTs coexpressed with an SGBP. RESULTS 168 190 glycan-importing TBDTs protein_type PUL-encoded TBDTs in Bacteroidetes are larger than the well-characterized iron-targeting TBDTs from many Proteobacteria and are further distinguished as the only known glycan-importing TBDTs coexpressed with an SGBP. RESULTS 211 215 SGBP protein_type PUL-encoded TBDTs in Bacteroidetes are larger than the well-characterized iron-targeting TBDTs from many Proteobacteria and are further distinguished as the only known glycan-importing TBDTs coexpressed with an SGBP. RESULTS 33 39 BtSusC protein A direct interaction between the BtSusC TBDT and the SusD SGBP has been previously demonstrated, as has an interaction between the homologous components encoded by an N-glycan-scavenging PUL of Capnocytophaga canimorsus. RESULTS 40 44 TBDT protein_type A direct interaction between the BtSusC TBDT and the SusD SGBP has been previously demonstrated, as has an interaction between the homologous components encoded by an N-glycan-scavenging PUL of Capnocytophaga canimorsus. RESULTS 53 57 SusD protein A direct interaction between the BtSusC TBDT and the SusD SGBP has been previously demonstrated, as has an interaction between the homologous components encoded by an N-glycan-scavenging PUL of Capnocytophaga canimorsus. RESULTS 58 62 SGBP protein_type A direct interaction between the BtSusC TBDT and the SusD SGBP has been previously demonstrated, as has an interaction between the homologous components encoded by an N-glycan-scavenging PUL of Capnocytophaga canimorsus. RESULTS 169 175 glycan chemical A direct interaction between the BtSusC TBDT and the SusD SGBP has been previously demonstrated, as has an interaction between the homologous components encoded by an N-glycan-scavenging PUL of Capnocytophaga canimorsus. RESULTS 187 190 PUL gene A direct interaction between the BtSusC TBDT and the SusD SGBP has been previously demonstrated, as has an interaction between the homologous components encoded by an N-glycan-scavenging PUL of Capnocytophaga canimorsus. RESULTS 194 219 Capnocytophaga canimorsus species A direct interaction between the BtSusC TBDT and the SusD SGBP has been previously demonstrated, as has an interaction between the homologous components encoded by an N-glycan-scavenging PUL of Capnocytophaga canimorsus. RESULTS 55 59 SusD protein Our observation here that the physical presence of the SusD homolog SGBP-A, independent of XyG-binding ability, is both necessary and sufficient for XyG utilization further supports a model of glycan import whereby the SusC-like TBDTs and the SusD-like SGBPs must be intimately associated to support glycan uptake (Fig. 1C). RESULTS 68 74 SGBP-A protein Our observation here that the physical presence of the SusD homolog SGBP-A, independent of XyG-binding ability, is both necessary and sufficient for XyG utilization further supports a model of glycan import whereby the SusC-like TBDTs and the SusD-like SGBPs must be intimately associated to support glycan uptake (Fig. 1C). RESULTS 91 94 XyG chemical Our observation here that the physical presence of the SusD homolog SGBP-A, independent of XyG-binding ability, is both necessary and sufficient for XyG utilization further supports a model of glycan import whereby the SusC-like TBDTs and the SusD-like SGBPs must be intimately associated to support glycan uptake (Fig. 1C). RESULTS 149 152 XyG chemical Our observation here that the physical presence of the SusD homolog SGBP-A, independent of XyG-binding ability, is both necessary and sufficient for XyG utilization further supports a model of glycan import whereby the SusC-like TBDTs and the SusD-like SGBPs must be intimately associated to support glycan uptake (Fig. 1C). RESULTS 193 199 glycan chemical Our observation here that the physical presence of the SusD homolog SGBP-A, independent of XyG-binding ability, is both necessary and sufficient for XyG utilization further supports a model of glycan import whereby the SusC-like TBDTs and the SusD-like SGBPs must be intimately associated to support glycan uptake (Fig. 1C). RESULTS 219 234 SusC-like TBDTs protein_type Our observation here that the physical presence of the SusD homolog SGBP-A, independent of XyG-binding ability, is both necessary and sufficient for XyG utilization further supports a model of glycan import whereby the SusC-like TBDTs and the SusD-like SGBPs must be intimately associated to support glycan uptake (Fig. 1C). RESULTS 243 258 SusD-like SGBPs protein_type Our observation here that the physical presence of the SusD homolog SGBP-A, independent of XyG-binding ability, is both necessary and sufficient for XyG utilization further supports a model of glycan import whereby the SusC-like TBDTs and the SusD-like SGBPs must be intimately associated to support glycan uptake (Fig. 1C). RESULTS 300 306 glycan chemical Our observation here that the physical presence of the SusD homolog SGBP-A, independent of XyG-binding ability, is both necessary and sufficient for XyG utilization further supports a model of glycan import whereby the SusC-like TBDTs and the SusD-like SGBPs must be intimately associated to support glycan uptake (Fig. 1C). RESULTS 120 124 TBDT protein_type It is yet presently unclear whether this interaction is static or dynamic and to what extent the association of cognate TBDT/SGBPs is dependent upon the structure of the carbohydrate to be imported. RESULTS 125 130 SGBPs protein_type It is yet presently unclear whether this interaction is static or dynamic and to what extent the association of cognate TBDT/SGBPs is dependent upon the structure of the carbohydrate to be imported. RESULTS 170 182 carbohydrate chemical It is yet presently unclear whether this interaction is static or dynamic and to what extent the association of cognate TBDT/SGBPs is dependent upon the structure of the carbohydrate to be imported. RESULTS 59 64 TBDTs protein_type On the other hand, there is clear evidence for independent TBDTs in Bacteroidetes that do not require SGBP association for activity. RESULTS 68 81 Bacteroidetes taxonomy_domain On the other hand, there is clear evidence for independent TBDTs in Bacteroidetes that do not require SGBP association for activity. RESULTS 102 106 SGBP protein_type On the other hand, there is clear evidence for independent TBDTs in Bacteroidetes that do not require SGBP association for activity. RESULTS 61 65 nanO gene For example, it was recently demonstrated that expression of nanO, which encodes a SusC-like TBDT as part of a sialic-acid-targeting PUL from B. fragilis, restored growth on this monosaccharide in a mutant strain of E. coli. RESULTS 83 97 SusC-like TBDT protein_type For example, it was recently demonstrated that expression of nanO, which encodes a SusC-like TBDT as part of a sialic-acid-targeting PUL from B. fragilis, restored growth on this monosaccharide in a mutant strain of E. coli. RESULTS 133 136 PUL gene For example, it was recently demonstrated that expression of nanO, which encodes a SusC-like TBDT as part of a sialic-acid-targeting PUL from B. fragilis, restored growth on this monosaccharide in a mutant strain of E. coli. RESULTS 142 153 B. fragilis species For example, it was recently demonstrated that expression of nanO, which encodes a SusC-like TBDT as part of a sialic-acid-targeting PUL from B. fragilis, restored growth on this monosaccharide in a mutant strain of E. coli. RESULTS 179 193 monosaccharide chemical For example, it was recently demonstrated that expression of nanO, which encodes a SusC-like TBDT as part of a sialic-acid-targeting PUL from B. fragilis, restored growth on this monosaccharide in a mutant strain of E. coli. RESULTS 216 223 E. coli species For example, it was recently demonstrated that expression of nanO, which encodes a SusC-like TBDT as part of a sialic-acid-targeting PUL from B. fragilis, restored growth on this monosaccharide in a mutant strain of E. coli. RESULTS 38 42 susD gene In this instance, coexpression of the susD-like gene nanU was not required, nor did the expression of the nanU gene enhance growth kinetics. RESULTS 53 57 nanU gene In this instance, coexpression of the susD-like gene nanU was not required, nor did the expression of the nanU gene enhance growth kinetics. RESULTS 106 110 nanU gene In this instance, coexpression of the susD-like gene nanU was not required, nor did the expression of the nanU gene enhance growth kinetics. RESULTS 27 33 BT1762 gene Similarly, the deletion of BT1762 encoding a fructan-targeting SusD-like protein in B. thetaiotaomicron did not result in a dramatic loss of growth on fructans. RESULTS 45 80 fructan-targeting SusD-like protein protein_type Similarly, the deletion of BT1762 encoding a fructan-targeting SusD-like protein in B. thetaiotaomicron did not result in a dramatic loss of growth on fructans. RESULTS 84 103 B. thetaiotaomicron species Similarly, the deletion of BT1762 encoding a fructan-targeting SusD-like protein in B. thetaiotaomicron did not result in a dramatic loss of growth on fructans. RESULTS 151 159 fructans chemical Similarly, the deletion of BT1762 encoding a fructan-targeting SusD-like protein in B. thetaiotaomicron did not result in a dramatic loss of growth on fructans. RESULTS 33 47 SusD-like SGBP protein_type Thus, the strict dependence on a SusD-like SGBP for glycan uptake in the Bacteroidetes may be variable and substrate dependent. RESULTS 52 58 glycan chemical Thus, the strict dependence on a SusD-like SGBP for glycan uptake in the Bacteroidetes may be variable and substrate dependent. RESULTS 73 86 Bacteroidetes taxonomy_domain Thus, the strict dependence on a SusD-like SGBP for glycan uptake in the Bacteroidetes may be variable and substrate dependent. RESULTS 53 58 TBDTs protein_type Furthermore, considering the broader distribution of TBDTs in PUL lacking SGBPs (sometimes known as carbohydrate utilization containing TBDT [CUT] loci; see reference and reviewed in reference) across bacterial phyla, it appears that the intimate biophysical association of these substrate-transport and -binding proteins is the result of specific evolution within the Bacteroidetes. RESULTS 62 65 PUL gene Furthermore, considering the broader distribution of TBDTs in PUL lacking SGBPs (sometimes known as carbohydrate utilization containing TBDT [CUT] loci; see reference and reviewed in reference) across bacterial phyla, it appears that the intimate biophysical association of these substrate-transport and -binding proteins is the result of specific evolution within the Bacteroidetes. RESULTS 74 79 SGBPs protein_type Furthermore, considering the broader distribution of TBDTs in PUL lacking SGBPs (sometimes known as carbohydrate utilization containing TBDT [CUT] loci; see reference and reviewed in reference) across bacterial phyla, it appears that the intimate biophysical association of these substrate-transport and -binding proteins is the result of specific evolution within the Bacteroidetes. RESULTS 100 151 carbohydrate utilization containing TBDT [CUT] loci gene Furthermore, considering the broader distribution of TBDTs in PUL lacking SGBPs (sometimes known as carbohydrate utilization containing TBDT [CUT] loci; see reference and reviewed in reference) across bacterial phyla, it appears that the intimate biophysical association of these substrate-transport and -binding proteins is the result of specific evolution within the Bacteroidetes. RESULTS 201 210 bacterial taxonomy_domain Furthermore, considering the broader distribution of TBDTs in PUL lacking SGBPs (sometimes known as carbohydrate utilization containing TBDT [CUT] loci; see reference and reviewed in reference) across bacterial phyla, it appears that the intimate biophysical association of these substrate-transport and -binding proteins is the result of specific evolution within the Bacteroidetes. RESULTS 369 382 Bacteroidetes taxonomy_domain Furthermore, considering the broader distribution of TBDTs in PUL lacking SGBPs (sometimes known as carbohydrate utilization containing TBDT [CUT] loci; see reference and reviewed in reference) across bacterial phyla, it appears that the intimate biophysical association of these substrate-transport and -binding proteins is the result of specific evolution within the Bacteroidetes. RESULTS 49 67 SusD-like proteins protein_type Equally intriguing is the observation that while SusD-like proteins such as SGBP-A share moderate primary and high tertiary structural conservation, the genes for the SGBPs encoded immediately downstream (Fig. 1B [sometimes referred to as “susE positioned”]) encode glycan-binding lipoproteins with little or no sequence or structural conservation, even among syntenic PUL that target the same polysaccharide. RESULTS 76 82 SGBP-A protein Equally intriguing is the observation that while SusD-like proteins such as SGBP-A share moderate primary and high tertiary structural conservation, the genes for the SGBPs encoded immediately downstream (Fig. 1B [sometimes referred to as “susE positioned”]) encode glycan-binding lipoproteins with little or no sequence or structural conservation, even among syntenic PUL that target the same polysaccharide. RESULTS 167 172 SGBPs protein_type Equally intriguing is the observation that while SusD-like proteins such as SGBP-A share moderate primary and high tertiary structural conservation, the genes for the SGBPs encoded immediately downstream (Fig. 1B [sometimes referred to as “susE positioned”]) encode glycan-binding lipoproteins with little or no sequence or structural conservation, even among syntenic PUL that target the same polysaccharide. RESULTS 266 293 glycan-binding lipoproteins protein_type Equally intriguing is the observation that while SusD-like proteins such as SGBP-A share moderate primary and high tertiary structural conservation, the genes for the SGBPs encoded immediately downstream (Fig. 1B [sometimes referred to as “susE positioned”]) encode glycan-binding lipoproteins with little or no sequence or structural conservation, even among syntenic PUL that target the same polysaccharide. RESULTS 369 372 PUL gene Equally intriguing is the observation that while SusD-like proteins such as SGBP-A share moderate primary and high tertiary structural conservation, the genes for the SGBPs encoded immediately downstream (Fig. 1B [sometimes referred to as “susE positioned”]) encode glycan-binding lipoproteins with little or no sequence or structural conservation, even among syntenic PUL that target the same polysaccharide. RESULTS 394 408 polysaccharide chemical Equally intriguing is the observation that while SusD-like proteins such as SGBP-A share moderate primary and high tertiary structural conservation, the genes for the SGBPs encoded immediately downstream (Fig. 1B [sometimes referred to as “susE positioned”]) encode glycan-binding lipoproteins with little or no sequence or structural conservation, even among syntenic PUL that target the same polysaccharide. RESULTS 21 26 XyGUL gene Such is the case for XyGUL from related Bacteroides species, which may encode either one or two of these predicted SGBPs, and these proteins vary considerably in length. RESULTS 40 51 Bacteroides taxonomy_domain Such is the case for XyGUL from related Bacteroides species, which may encode either one or two of these predicted SGBPs, and these proteins vary considerably in length. RESULTS 115 120 SGBPs protein_type Such is the case for XyGUL from related Bacteroides species, which may encode either one or two of these predicted SGBPs, and these proteins vary considerably in length. RESULTS 38 43 SGBPs protein_type The extremely low similarity of these SGBPs is striking in light of the moderate sequence conservation observed among homologous GHs in syntenic PUL. RESULTS 129 132 GHs protein_type The extremely low similarity of these SGBPs is striking in light of the moderate sequence conservation observed among homologous GHs in syntenic PUL. RESULTS 145 148 PUL gene The extremely low similarity of these SGBPs is striking in light of the moderate sequence conservation observed among homologous GHs in syntenic PUL. RESULTS 47 52 SGBPs protein_type This, together with the observation that these SGBPs, as exemplified by BtSusE and BtSusF and the XyGUL SGBP-B of the present study, are expendable for polysaccharide growth, implies a high degree of evolutionary flexibility to enhance glycan capture at the cell surface. RESULTS 72 78 BtSusE protein This, together with the observation that these SGBPs, as exemplified by BtSusE and BtSusF and the XyGUL SGBP-B of the present study, are expendable for polysaccharide growth, implies a high degree of evolutionary flexibility to enhance glycan capture at the cell surface. RESULTS 83 89 BtSusF protein This, together with the observation that these SGBPs, as exemplified by BtSusE and BtSusF and the XyGUL SGBP-B of the present study, are expendable for polysaccharide growth, implies a high degree of evolutionary flexibility to enhance glycan capture at the cell surface. RESULTS 98 103 XyGUL gene This, together with the observation that these SGBPs, as exemplified by BtSusE and BtSusF and the XyGUL SGBP-B of the present study, are expendable for polysaccharide growth, implies a high degree of evolutionary flexibility to enhance glycan capture at the cell surface. RESULTS 104 110 SGBP-B protein This, together with the observation that these SGBPs, as exemplified by BtSusE and BtSusF and the XyGUL SGBP-B of the present study, are expendable for polysaccharide growth, implies a high degree of evolutionary flexibility to enhance glycan capture at the cell surface. RESULTS 152 166 polysaccharide chemical This, together with the observation that these SGBPs, as exemplified by BtSusE and BtSusF and the XyGUL SGBP-B of the present study, are expendable for polysaccharide growth, implies a high degree of evolutionary flexibility to enhance glycan capture at the cell surface. RESULTS 236 242 glycan chemical This, together with the observation that these SGBPs, as exemplified by BtSusE and BtSusF and the XyGUL SGBP-B of the present study, are expendable for polysaccharide growth, implies a high degree of evolutionary flexibility to enhance glycan capture at the cell surface. RESULTS 58 66 bacteria taxonomy_domain Because the intestinal ecosystem is a dense consortium of bacteria that must compete for their nutrients, these multimodular SGBPs may reflect ongoing evolutionary experiments to enhance glycan uptake efficiency. RESULTS 125 130 SGBPs protein_type Because the intestinal ecosystem is a dense consortium of bacteria that must compete for their nutrients, these multimodular SGBPs may reflect ongoing evolutionary experiments to enhance glycan uptake efficiency. RESULTS 187 193 glycan chemical Because the intestinal ecosystem is a dense consortium of bacteria that must compete for their nutrients, these multimodular SGBPs may reflect ongoing evolutionary experiments to enhance glycan uptake efficiency. RESULTS 38 43 SGBPs protein_type Whether organisms that express longer SGBPs, extending further above the cell surface toward the extracellular environment, are better equipped to compete for available carbohydrates is presently unknown. RESULTS 169 182 carbohydrates chemical Whether organisms that express longer SGBPs, extending further above the cell surface toward the extracellular environment, are better equipped to compete for available carbohydrates is presently unknown. RESULTS 102 129 carbohydrate-binding motifs structure_element However, the natural diversity of these proteins represents a rich source for the discovery of unique carbohydrate-binding motifs to both inform gut microbiology and generate new, specific carbohydrate analytical reagents. RESULTS 189 201 carbohydrate chemical However, the natural diversity of these proteins represents a rich source for the discovery of unique carbohydrate-binding motifs to both inform gut microbiology and generate new, specific carbohydrate analytical reagents. RESULTS 77 108 surface-glycan binding proteins protein_type In conclusion, the present study further illuminates the essential role that surface-glycan binding proteins play in facilitating the catabolism of complex dietary carbohydrates by Bacteroidetes. RESULTS 164 177 carbohydrates chemical In conclusion, the present study further illuminates the essential role that surface-glycan binding proteins play in facilitating the catabolism of complex dietary carbohydrates by Bacteroidetes. RESULTS 181 194 Bacteroidetes taxonomy_domain In conclusion, the present study further illuminates the essential role that surface-glycan binding proteins play in facilitating the catabolism of complex dietary carbohydrates by Bacteroidetes. RESULTS 32 40 bacteria taxonomy_domain The ability of our resident gut bacteria to recognize polysaccharides is the first committed step of glycan consumption by these organisms, a critical process that influences the community structure and thus the metabolic output (i.e., short-chain fatty acid and metabolite profile) of these organisms. RESULTS 54 69 polysaccharides chemical The ability of our resident gut bacteria to recognize polysaccharides is the first committed step of glycan consumption by these organisms, a critical process that influences the community structure and thus the metabolic output (i.e., short-chain fatty acid and metabolite profile) of these organisms. RESULTS 101 107 glycan chemical The ability of our resident gut bacteria to recognize polysaccharides is the first committed step of glycan consumption by these organisms, a critical process that influences the community structure and thus the metabolic output (i.e., short-chain fatty acid and metabolite profile) of these organisms. RESULTS 29 35 glycan chemical A molecular understanding of glycan uptake by human gut bacteria is therefore central to the development of strategies to improve human health through manipulation of the microbiota. RESULTS 46 51 human species A molecular understanding of glycan uptake by human gut bacteria is therefore central to the development of strategies to improve human health through manipulation of the microbiota. RESULTS 56 64 bacteria taxonomy_domain A molecular understanding of glycan uptake by human gut bacteria is therefore central to the development of strategies to improve human health through manipulation of the microbiota. RESULTS 130 135 human species A molecular understanding of glycan uptake by human gut bacteria is therefore central to the development of strategies to improve human health through manipulation of the microbiota. RESULTS 171 181 microbiota taxonomy_domain A molecular understanding of glycan uptake by human gut bacteria is therefore central to the development of strategies to improve human health through manipulation of the microbiota. RESULTS 8 14 glycan chemical Mucosal glycan foraging enhances fitness and transmission of a saccharolytic human gut bacterial symbiont REF