| anno_start anno_end anno_text entity_type sentence section | |
| 4 11 dynamic protein_state The dynamic organization of fungal acetyl-CoA carboxylase TITLE | |
| 28 34 fungal taxonomy_domain The dynamic organization of fungal acetyl-CoA carboxylase TITLE | |
| 35 57 acetyl-CoA carboxylase protein_type The dynamic organization of fungal acetyl-CoA carboxylase TITLE | |
| 0 23 Acetyl-CoA carboxylases protein_type Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of the metabolic syndrome and cancer. ABSTRACT | |
| 25 29 ACCs protein_type Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of the metabolic syndrome and cancer. ABSTRACT | |
| 91 94 ATP chemical Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of the metabolic syndrome and cancer. ABSTRACT | |
| 122 132 acetyl-CoA chemical Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of the metabolic syndrome and cancer. ABSTRACT | |
| 136 147 malonyl-CoA chemical Acetyl-CoA carboxylases (ACCs) catalyse the committed step in fatty-acid biosynthesis: the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. They are important regulatory hubs for metabolic control and relevant drug targets for the treatment of the metabolic syndrome and cancer. ABSTRACT | |
| 0 10 Eukaryotic taxonomy_domain Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. ABSTRACT | |
| 11 15 ACCs protein_type Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. ABSTRACT | |
| 20 45 single-chain multienzymes protein_type Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. ABSTRACT | |
| 72 85 non-catalytic protein_state Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. ABSTRACT | |
| 86 100 central domain structure_element Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. ABSTRACT | |
| 102 104 CD structure_element Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. ABSTRACT | |
| 121 124 ACC protein_type Eukaryotic ACCs are single-chain multienzymes characterized by a large, non-catalytic central domain (CD), whose role in ACC regulation remains poorly characterized. ABSTRACT | |
| 19 36 crystal structure evidence Here we report the crystal structure of the yeast ACC CD, revealing a unique four-domain organization. ABSTRACT | |
| 44 49 yeast taxonomy_domain Here we report the crystal structure of the yeast ACC CD, revealing a unique four-domain organization. ABSTRACT | |
| 50 53 ACC protein_type Here we report the crystal structure of the yeast ACC CD, revealing a unique four-domain organization. ABSTRACT | |
| 54 56 CD structure_element Here we report the crystal structure of the yeast ACC CD, revealing a unique four-domain organization. ABSTRACT | |
| 2 17 regulatory loop structure_element A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. ABSTRACT | |
| 28 42 phosphorylated protein_state A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. ABSTRACT | |
| 65 85 phosphorylation site site A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. ABSTRACT | |
| 89 95 fungal taxonomy_domain A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. ABSTRACT | |
| 96 99 ACC protein_type A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. ABSTRACT | |
| 146 148 CD structure_element A regulatory loop, which is phosphorylated at the key functional phosphorylation site of fungal ACC, wedges into a crevice between two domains of CD. ABSTRACT | |
| 14 19 yeast taxonomy_domain Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 20 22 CD structure_element Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 23 32 structure evidence Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 78 94 larger fragments mutant Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 101 107 intact protein_state Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 108 112 ACCs protein_type Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 162 169 dynamic protein_state Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 170 176 fungal taxonomy_domain Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 177 180 ACC protein_type Combining the yeast CD structure with intermediate and low-resolution data of larger fragments up to intact ACCs provides a comprehensive characterization of the dynamic fungal ACC architecture. ABSTRACT | |
| 23 35 carboxylases protein_type In contrast to related carboxylases, large-scale conformational changes are required for substrate turnover, and are mediated by the CD under phosphorylation control. ABSTRACT | |
| 133 135 CD structure_element In contrast to related carboxylases, large-scale conformational changes are required for substrate turnover, and are mediated by the CD under phosphorylation control. ABSTRACT | |
| 142 157 phosphorylation ptm In contrast to related carboxylases, large-scale conformational changes are required for substrate turnover, and are mediated by the CD under phosphorylation control. ABSTRACT | |
| 1 24 Acetyl-CoA carboxylases protein_type Acetyl-CoA carboxylases are central regulatory hubs of fatty acid metabolism and are important targets for drug development in obesity and cancer. ABSTRACT | |
| 59 73 highly dynamic protein_state Here, the authors demonstrate that the regulation of these highly dynamic enzymes in fungi is governed by a mechanism based on phosphorylation-dependent conformational variability. ABSTRACT | |
| 74 81 enzymes protein_type Here, the authors demonstrate that the regulation of these highly dynamic enzymes in fungi is governed by a mechanism based on phosphorylation-dependent conformational variability. ABSTRACT | |
| 85 90 fungi taxonomy_domain Here, the authors demonstrate that the regulation of these highly dynamic enzymes in fungi is governed by a mechanism based on phosphorylation-dependent conformational variability. ABSTRACT | |
| 127 142 phosphorylation ptm Here, the authors demonstrate that the regulation of these highly dynamic enzymes in fungi is governed by a mechanism based on phosphorylation-dependent conformational variability. ABSTRACT | |
| 0 40 Biotin-dependent acetyl-CoA carboxylases protein_type Biotin-dependent acetyl-CoA carboxylases (ACCs) are essential enzymes that catalyse the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. This reaction provides the committed activated substrate for the biosynthesis of fatty acids via fatty-acid synthase. INTRO | |
| 42 46 ACCs protein_type Biotin-dependent acetyl-CoA carboxylases (ACCs) are essential enzymes that catalyse the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. This reaction provides the committed activated substrate for the biosynthesis of fatty acids via fatty-acid synthase. INTRO | |
| 88 91 ATP chemical Biotin-dependent acetyl-CoA carboxylases (ACCs) are essential enzymes that catalyse the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. This reaction provides the committed activated substrate for the biosynthesis of fatty acids via fatty-acid synthase. INTRO | |
| 119 129 acetyl-CoA chemical Biotin-dependent acetyl-CoA carboxylases (ACCs) are essential enzymes that catalyse the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. This reaction provides the committed activated substrate for the biosynthesis of fatty acids via fatty-acid synthase. INTRO | |
| 133 144 malonyl-CoA chemical Biotin-dependent acetyl-CoA carboxylases (ACCs) are essential enzymes that catalyse the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. This reaction provides the committed activated substrate for the biosynthesis of fatty acids via fatty-acid synthase. INTRO | |
| 227 238 fatty acids chemical Biotin-dependent acetyl-CoA carboxylases (ACCs) are essential enzymes that catalyse the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. This reaction provides the committed activated substrate for the biosynthesis of fatty acids via fatty-acid synthase. INTRO | |
| 243 262 fatty-acid synthase protein_type Biotin-dependent acetyl-CoA carboxylases (ACCs) are essential enzymes that catalyse the ATP-dependent carboxylation of acetyl-CoA to malonyl-CoA. This reaction provides the committed activated substrate for the biosynthesis of fatty acids via fatty-acid synthase. INTRO | |
| 66 69 ACC protein_type By catalysing this rate-limiting step in fatty-acid biosynthesis, ACC plays a key role in anabolic metabolism. INTRO | |
| 0 36 ACC inhibition and knock-out studies experimental_method ACC inhibition and knock-out studies show the potential of targeting ACC for treatment of the metabolic syndrome. INTRO | |
| 69 72 ACC protein_type ACC inhibition and knock-out studies show the potential of targeting ACC for treatment of the metabolic syndrome. INTRO | |
| 22 25 ACC protein_type Furthermore, elevated ACC activity is observed in malignant tumours. INTRO | |
| 22 25 ACC protein_type A direct link between ACC and cancer is provided by cancer-associated mutations in the breast cancer susceptibility gene 1 (BRCA1), which relieve inhibitory interactions of BRCA1 with ACC. INTRO | |
| 70 79 mutations mutant A direct link between ACC and cancer is provided by cancer-associated mutations in the breast cancer susceptibility gene 1 (BRCA1), which relieve inhibitory interactions of BRCA1 with ACC. INTRO | |
| 87 122 breast cancer susceptibility gene 1 protein A direct link between ACC and cancer is provided by cancer-associated mutations in the breast cancer susceptibility gene 1 (BRCA1), which relieve inhibitory interactions of BRCA1 with ACC. INTRO | |
| 124 129 BRCA1 protein A direct link between ACC and cancer is provided by cancer-associated mutations in the breast cancer susceptibility gene 1 (BRCA1), which relieve inhibitory interactions of BRCA1 with ACC. INTRO | |
| 173 178 BRCA1 protein A direct link between ACC and cancer is provided by cancer-associated mutations in the breast cancer susceptibility gene 1 (BRCA1), which relieve inhibitory interactions of BRCA1 with ACC. INTRO | |
| 184 187 ACC protein_type A direct link between ACC and cancer is provided by cancer-associated mutations in the breast cancer susceptibility gene 1 (BRCA1), which relieve inhibitory interactions of BRCA1 with ACC. INTRO | |
| 6 9 ACC protein_type Thus, ACC is a relevant drug target for type 2 diabetes and cancer. INTRO | |
| 0 9 Microbial taxonomy_domain Microbial ACCs are also the principal target of antifungal and antibiotic compounds, such as Soraphen A. INTRO | |
| 10 14 ACCs protein_type Microbial ACCs are also the principal target of antifungal and antibiotic compounds, such as Soraphen A. INTRO | |
| 93 103 Soraphen A chemical Microbial ACCs are also the principal target of antifungal and antibiotic compounds, such as Soraphen A. INTRO | |
| 47 51 ACCs protein_type The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 102 118 Escherichia coli species The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 120 127 E. coli species The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 129 132 ACC protein_type The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 134 152 Biotin carboxylase protein_type The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 154 156 BC protein_type The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 172 175 ATP chemical The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 205 211 biotin chemical The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 254 285 biotin carboxyl carrier protein protein_type The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 287 291 BCCP protein_type The principal functional protein components of ACCs have been described already in the late 1960s for Escherichia coli (E. coli) ACC: Biotin carboxylase (BC) catalyses the ATP-dependent carboxylation of a biotin moiety, which is covalently linked to the biotin carboxyl carrier protein (BCCP). INTRO | |
| 0 19 Carboxyltransferase protein_type Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 21 23 CT protein_type Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 49 57 carboxyl chemical Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 69 82 carboxybiotin chemical Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 86 96 acetyl-CoA chemical Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 106 117 malonyl-CoA chemical Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 119 130 Prokaryotic taxonomy_domain Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 131 135 ACCs protein_type Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 140 149 transient protein_state Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 175 177 BC protein_type Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 179 181 CT protein_type Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 186 190 BCCP protein_type Carboxyltransferase (CT) transfers the activated carboxyl group from carboxybiotin to acetyl-CoA to yield malonyl-CoA. Prokaryotic ACCs are transient assemblies of individual BC, CT and BCCP subunits. INTRO | |
| 0 10 Eukaryotic taxonomy_domain Eukaryotic ACCs, instead, are multienzymes, which integrate all functional components into a single polypeptide chain of ∼2,300 amino acids. INTRO | |
| 11 15 ACCs protein_type Eukaryotic ACCs, instead, are multienzymes, which integrate all functional components into a single polypeptide chain of ∼2,300 amino acids. INTRO | |
| 30 42 multienzymes protein_type Eukaryotic ACCs, instead, are multienzymes, which integrate all functional components into a single polypeptide chain of ∼2,300 amino acids. INTRO | |
| 0 5 Human species Human ACC occurs in two closely related isoforms, ACC1 and 2, located in the cytosol and at the outer mitochondrial membrane, respectively. INTRO | |
| 6 9 ACC protein_type Human ACC occurs in two closely related isoforms, ACC1 and 2, located in the cytosol and at the outer mitochondrial membrane, respectively. INTRO | |
| 40 48 isoforms protein_state Human ACC occurs in two closely related isoforms, ACC1 and 2, located in the cytosol and at the outer mitochondrial membrane, respectively. INTRO | |
| 50 54 ACC1 protein Human ACC occurs in two closely related isoforms, ACC1 and 2, located in the cytosol and at the outer mitochondrial membrane, respectively. INTRO | |
| 59 60 2 protein Human ACC occurs in two closely related isoforms, ACC1 and 2, located in the cytosol and at the outer mitochondrial membrane, respectively. INTRO | |
| 29 43 ACC components structure_element In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 45 55 eukaryotic taxonomy_domain In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 56 60 ACCs protein_type In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 73 86 non-catalytic protein_state In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 87 94 regions structure_element In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 106 120 central domain structure_element In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 122 124 CD structure_element In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 134 158 BC–CT interaction domain structure_element In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 160 162 BT structure_element In addition to the canonical ACC components, eukaryotic ACCs contain two non-catalytic regions, the large central domain (CD) and the BC–CT interaction domain (BT). INTRO | |
| 4 6 CD structure_element The CD comprises one-third of the protein and is a unique feature of eukaryotic ACCs without homologues in other proteins. INTRO | |
| 51 68 unique feature of protein_state The CD comprises one-third of the protein and is a unique feature of eukaryotic ACCs without homologues in other proteins. INTRO | |
| 69 79 eukaryotic taxonomy_domain The CD comprises one-third of the protein and is a unique feature of eukaryotic ACCs without homologues in other proteins. INTRO | |
| 80 84 ACCs protein_type The CD comprises one-third of the protein and is a unique feature of eukaryotic ACCs without homologues in other proteins. INTRO | |
| 67 82 phosphorylation ptm The function of this domain remains poorly characterized, although phosphorylation of several serine residues in the CD regulates ACC activity. INTRO | |
| 94 100 serine residue_name The function of this domain remains poorly characterized, although phosphorylation of several serine residues in the CD regulates ACC activity. INTRO | |
| 117 119 CD structure_element The function of this domain remains poorly characterized, although phosphorylation of several serine residues in the CD regulates ACC activity. INTRO | |
| 130 133 ACC protein_type The function of this domain remains poorly characterized, although phosphorylation of several serine residues in the CD regulates ACC activity. INTRO | |
| 4 6 BT structure_element The BT domain has been visualized in bacterial carboxylases, where it mediates contacts between α- and β-subunits. INTRO | |
| 37 46 bacterial taxonomy_domain The BT domain has been visualized in bacterial carboxylases, where it mediates contacts between α- and β-subunits. INTRO | |
| 47 59 carboxylases protein_type The BT domain has been visualized in bacterial carboxylases, where it mediates contacts between α- and β-subunits. INTRO | |
| 96 98 α- structure_element The BT domain has been visualized in bacterial carboxylases, where it mediates contacts between α- and β-subunits. INTRO | |
| 103 113 β-subunits structure_element The BT domain has been visualized in bacterial carboxylases, where it mediates contacts between α- and β-subunits. INTRO | |
| 0 18 Structural studies experimental_method Structural studies on the functional architecture of intact ACCs have been hindered by their huge size and pronounced dynamics, as well as the transient assembly mode of bacterial ACCs. INTRO | |
| 53 59 intact protein_state Structural studies on the functional architecture of intact ACCs have been hindered by their huge size and pronounced dynamics, as well as the transient assembly mode of bacterial ACCs. INTRO | |
| 60 64 ACCs protein_type Structural studies on the functional architecture of intact ACCs have been hindered by their huge size and pronounced dynamics, as well as the transient assembly mode of bacterial ACCs. INTRO | |
| 143 152 transient protein_state Structural studies on the functional architecture of intact ACCs have been hindered by their huge size and pronounced dynamics, as well as the transient assembly mode of bacterial ACCs. INTRO | |
| 170 179 bacterial taxonomy_domain Structural studies on the functional architecture of intact ACCs have been hindered by their huge size and pronounced dynamics, as well as the transient assembly mode of bacterial ACCs. INTRO | |
| 180 184 ACCs protein_type Structural studies on the functional architecture of intact ACCs have been hindered by their huge size and pronounced dynamics, as well as the transient assembly mode of bacterial ACCs. INTRO | |
| 9 27 crystal structures evidence However, crystal structures of individual components or domains from prokaryotic and eukaryotic ACCs, respectively, have been solved. INTRO | |
| 69 80 prokaryotic taxonomy_domain However, crystal structures of individual components or domains from prokaryotic and eukaryotic ACCs, respectively, have been solved. INTRO | |
| 85 95 eukaryotic taxonomy_domain However, crystal structures of individual components or domains from prokaryotic and eukaryotic ACCs, respectively, have been solved. INTRO | |
| 96 100 ACCs protein_type However, crystal structures of individual components or domains from prokaryotic and eukaryotic ACCs, respectively, have been solved. INTRO | |
| 4 27 structure determination experimental_method The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 35 46 holoenzymes protein_state The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 50 59 bacterial taxonomy_domain The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 60 89 biotin-dependent carboxylases protein_type The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 97 101 lack protein_state The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 121 123 CD structure_element The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 137 157 pyruvate carboxylase protein_type The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 159 161 PC protein_type The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 164 189 propionyl-CoA carboxylase protein_type The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 191 224 3-methyl-crotonyl-CoA carboxylase protein_type The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 231 262 long-chain acyl-CoA carboxylase protein_type The structure determination of the holoenzymes of bacterial biotin-dependent carboxylases, which lack the characteristic CD, such as the pyruvate carboxylase (PC), propionyl-CoA carboxylase, 3-methyl-crotonyl-CoA carboxylase and a long-chain acyl-CoA carboxylase revealed strikingly divergent architectures despite a general conservation of all functional components. INTRO | |
| 9 19 structures evidence In these structures, the BC and CT active sites are at distances between 40 and 80 Å, such that substrate transfer could be mediated solely by the mobility of the flexibly tethered BCCP. INTRO | |
| 25 27 BC protein_type In these structures, the BC and CT active sites are at distances between 40 and 80 Å, such that substrate transfer could be mediated solely by the mobility of the flexibly tethered BCCP. INTRO | |
| 32 34 CT protein_type In these structures, the BC and CT active sites are at distances between 40 and 80 Å, such that substrate transfer could be mediated solely by the mobility of the flexibly tethered BCCP. INTRO | |
| 35 47 active sites site In these structures, the BC and CT active sites are at distances between 40 and 80 Å, such that substrate transfer could be mediated solely by the mobility of the flexibly tethered BCCP. INTRO | |
| 163 180 flexibly tethered protein_state In these structures, the BC and CT active sites are at distances between 40 and 80 Å, such that substrate transfer could be mediated solely by the mobility of the flexibly tethered BCCP. INTRO | |
| 181 185 BCCP protein_type In these structures, the BC and CT active sites are at distances between 40 and 80 Å, such that substrate transfer could be mediated solely by the mobility of the flexibly tethered BCCP. INTRO | |
| 0 5 Human species Human ACC1 is regulated allosterically, via specific protein–protein interactions, and by reversible phosphorylation. INTRO | |
| 6 10 ACC1 protein Human ACC1 is regulated allosterically, via specific protein–protein interactions, and by reversible phosphorylation. INTRO | |
| 14 38 regulated allosterically protein_state Human ACC1 is regulated allosterically, via specific protein–protein interactions, and by reversible phosphorylation. INTRO | |
| 101 116 phosphorylation ptm Human ACC1 is regulated allosterically, via specific protein–protein interactions, and by reversible phosphorylation. INTRO | |
| 26 31 human species Dynamic polymerization of human ACC1 is linked to increased activity and is regulated allosterically by the activator citrate and the inhibitor palmitate, or by binding of the small protein MIG-12 (ref.). INTRO | |
| 32 36 ACC1 protein Dynamic polymerization of human ACC1 is linked to increased activity and is regulated allosterically by the activator citrate and the inhibitor palmitate, or by binding of the small protein MIG-12 (ref.). INTRO | |
| 76 100 regulated allosterically protein_state Dynamic polymerization of human ACC1 is linked to increased activity and is regulated allosterically by the activator citrate and the inhibitor palmitate, or by binding of the small protein MIG-12 (ref.). INTRO | |
| 118 125 citrate chemical Dynamic polymerization of human ACC1 is linked to increased activity and is regulated allosterically by the activator citrate and the inhibitor palmitate, or by binding of the small protein MIG-12 (ref.). INTRO | |
| 144 153 palmitate chemical Dynamic polymerization of human ACC1 is linked to increased activity and is regulated allosterically by the activator citrate and the inhibitor palmitate, or by binding of the small protein MIG-12 (ref.). INTRO | |
| 190 196 MIG-12 protein Dynamic polymerization of human ACC1 is linked to increased activity and is regulated allosterically by the activator citrate and the inhibitor palmitate, or by binding of the small protein MIG-12 (ref.). INTRO | |
| 0 5 Human species Human ACC1 is further regulated by specific phosphorylation-dependent binding of BRCA1 to Ser1263 in the CD. INTRO | |
| 6 10 ACC1 protein Human ACC1 is further regulated by specific phosphorylation-dependent binding of BRCA1 to Ser1263 in the CD. INTRO | |
| 44 59 phosphorylation ptm Human ACC1 is further regulated by specific phosphorylation-dependent binding of BRCA1 to Ser1263 in the CD. INTRO | |
| 81 86 BRCA1 protein Human ACC1 is further regulated by specific phosphorylation-dependent binding of BRCA1 to Ser1263 in the CD. INTRO | |
| 90 97 Ser1263 residue_name_number Human ACC1 is further regulated by specific phosphorylation-dependent binding of BRCA1 to Ser1263 in the CD. INTRO | |
| 105 107 CD structure_element Human ACC1 is further regulated by specific phosphorylation-dependent binding of BRCA1 to Ser1263 in the CD. INTRO | |
| 0 5 BRCA1 protein BRCA1 binds only to the phosphorylated form of ACC1 and prevents ACC activation by phosphatase-mediated dephosphorylation. INTRO | |
| 24 38 phosphorylated protein_state BRCA1 binds only to the phosphorylated form of ACC1 and prevents ACC activation by phosphatase-mediated dephosphorylation. INTRO | |
| 47 51 ACC1 protein BRCA1 binds only to the phosphorylated form of ACC1 and prevents ACC activation by phosphatase-mediated dephosphorylation. INTRO | |
| 65 68 ACC protein_type BRCA1 binds only to the phosphorylated form of ACC1 and prevents ACC activation by phosphatase-mediated dephosphorylation. INTRO | |
| 83 94 phosphatase protein_type BRCA1 binds only to the phosphorylated form of ACC1 and prevents ACC activation by phosphatase-mediated dephosphorylation. INTRO | |
| 13 28 phosphorylation ptm Furthermore, phosphorylation by AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (PKA) leads to a decrease in ACC1 activity. INTRO | |
| 32 60 AMP-activated protein kinase protein Furthermore, phosphorylation by AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (PKA) leads to a decrease in ACC1 activity. INTRO | |
| 62 66 AMPK protein Furthermore, phosphorylation by AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (PKA) leads to a decrease in ACC1 activity. INTRO | |
| 72 101 cAMP-dependent protein kinase protein Furthermore, phosphorylation by AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (PKA) leads to a decrease in ACC1 activity. INTRO | |
| 103 106 PKA protein Furthermore, phosphorylation by AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (PKA) leads to a decrease in ACC1 activity. INTRO | |
| 131 135 ACC1 protein Furthermore, phosphorylation by AMP-activated protein kinase (AMPK) and cAMP-dependent protein kinase (PKA) leads to a decrease in ACC1 activity. INTRO | |
| 0 4 AMPK protein AMPK phosphorylates ACC1 in vitro at Ser80, Ser1201 and Ser1216 and PKA at Ser78 and Ser1201. INTRO | |
| 20 24 ACC1 protein AMPK phosphorylates ACC1 in vitro at Ser80, Ser1201 and Ser1216 and PKA at Ser78 and Ser1201. INTRO | |
| 37 42 Ser80 residue_name_number AMPK phosphorylates ACC1 in vitro at Ser80, Ser1201 and Ser1216 and PKA at Ser78 and Ser1201. INTRO | |
| 44 51 Ser1201 residue_name_number AMPK phosphorylates ACC1 in vitro at Ser80, Ser1201 and Ser1216 and PKA at Ser78 and Ser1201. INTRO | |
| 56 63 Ser1216 residue_name_number AMPK phosphorylates ACC1 in vitro at Ser80, Ser1201 and Ser1216 and PKA at Ser78 and Ser1201. INTRO | |
| 68 71 PKA protein AMPK phosphorylates ACC1 in vitro at Ser80, Ser1201 and Ser1216 and PKA at Ser78 and Ser1201. INTRO | |
| 75 80 Ser78 residue_name_number AMPK phosphorylates ACC1 in vitro at Ser80, Ser1201 and Ser1216 and PKA at Ser78 and Ser1201. INTRO | |
| 85 92 Ser1201 residue_name_number AMPK phosphorylates ACC1 in vitro at Ser80, Ser1201 and Ser1216 and PKA at Ser78 and Ser1201. INTRO | |
| 31 35 ACC1 protein However, regulatory effects on ACC1 activity are mainly mediated by phosphorylation of Ser80 and Ser1201 (refs). INTRO | |
| 68 83 phosphorylation ptm However, regulatory effects on ACC1 activity are mainly mediated by phosphorylation of Ser80 and Ser1201 (refs). INTRO | |
| 87 92 Ser80 residue_name_number However, regulatory effects on ACC1 activity are mainly mediated by phosphorylation of Ser80 and Ser1201 (refs). INTRO | |
| 97 104 Ser1201 residue_name_number However, regulatory effects on ACC1 activity are mainly mediated by phosphorylation of Ser80 and Ser1201 (refs). INTRO | |
| 0 14 Phosphorylated protein_state Phosphorylated Ser80, which is highly conserved only in higher eukaryotes, presumably binds into the Soraphen A-binding pocket. INTRO | |
| 15 20 Ser80 residue_name_number Phosphorylated Ser80, which is highly conserved only in higher eukaryotes, presumably binds into the Soraphen A-binding pocket. INTRO | |
| 31 47 highly conserved protein_state Phosphorylated Ser80, which is highly conserved only in higher eukaryotes, presumably binds into the Soraphen A-binding pocket. INTRO | |
| 56 73 higher eukaryotes taxonomy_domain Phosphorylated Ser80, which is highly conserved only in higher eukaryotes, presumably binds into the Soraphen A-binding pocket. INTRO | |
| 101 126 Soraphen A-binding pocket site Phosphorylated Ser80, which is highly conserved only in higher eukaryotes, presumably binds into the Soraphen A-binding pocket. INTRO | |
| 15 22 Ser1201 residue_name_number The regulatory Ser1201 shows only moderate conservation across higher eukaryotes, while the phosphorylated Ser1216 is highly conserved across all eukaryotes. INTRO | |
| 34 55 moderate conservation protein_state The regulatory Ser1201 shows only moderate conservation across higher eukaryotes, while the phosphorylated Ser1216 is highly conserved across all eukaryotes. INTRO | |
| 63 80 higher eukaryotes taxonomy_domain The regulatory Ser1201 shows only moderate conservation across higher eukaryotes, while the phosphorylated Ser1216 is highly conserved across all eukaryotes. INTRO | |
| 92 106 phosphorylated protein_state The regulatory Ser1201 shows only moderate conservation across higher eukaryotes, while the phosphorylated Ser1216 is highly conserved across all eukaryotes. INTRO | |
| 107 114 Ser1216 residue_name_number The regulatory Ser1201 shows only moderate conservation across higher eukaryotes, while the phosphorylated Ser1216 is highly conserved across all eukaryotes. INTRO | |
| 118 134 highly conserved protein_state The regulatory Ser1201 shows only moderate conservation across higher eukaryotes, while the phosphorylated Ser1216 is highly conserved across all eukaryotes. INTRO | |
| 146 156 eukaryotes taxonomy_domain The regulatory Ser1201 shows only moderate conservation across higher eukaryotes, while the phosphorylated Ser1216 is highly conserved across all eukaryotes. INTRO | |
| 22 29 Ser1216 residue_name_number However, no effect of Ser1216 phosphorylation on ACC activity has been reported in higher eukaryotes. INTRO | |
| 30 45 phosphorylation ptm However, no effect of Ser1216 phosphorylation on ACC activity has been reported in higher eukaryotes. INTRO | |
| 49 52 ACC protein_type However, no effect of Ser1216 phosphorylation on ACC activity has been reported in higher eukaryotes. INTRO | |
| 83 100 higher eukaryotes taxonomy_domain However, no effect of Ser1216 phosphorylation on ACC activity has been reported in higher eukaryotes. INTRO | |
| 4 10 fungal taxonomy_domain For fungal ACC, neither spontaneous nor inducible polymerization has been detected despite considerable sequence conservation to human ACC1. INTRO | |
| 11 14 ACC protein_type For fungal ACC, neither spontaneous nor inducible polymerization has been detected despite considerable sequence conservation to human ACC1. INTRO | |
| 129 134 human species For fungal ACC, neither spontaneous nor inducible polymerization has been detected despite considerable sequence conservation to human ACC1. INTRO | |
| 135 139 ACC1 protein For fungal ACC, neither spontaneous nor inducible polymerization has been detected despite considerable sequence conservation to human ACC1. INTRO | |
| 4 9 BRCA1 protein The BRCA1-interacting phosphoserine position is not conserved in fungal ACC, and no other phospho-dependent protein–protein interactions of fungal ACC have been described. INTRO | |
| 22 35 phosphoserine residue_name The BRCA1-interacting phosphoserine position is not conserved in fungal ACC, and no other phospho-dependent protein–protein interactions of fungal ACC have been described. INTRO | |
| 48 61 not conserved protein_state The BRCA1-interacting phosphoserine position is not conserved in fungal ACC, and no other phospho-dependent protein–protein interactions of fungal ACC have been described. INTRO | |
| 65 71 fungal taxonomy_domain The BRCA1-interacting phosphoserine position is not conserved in fungal ACC, and no other phospho-dependent protein–protein interactions of fungal ACC have been described. INTRO | |
| 72 75 ACC protein_type The BRCA1-interacting phosphoserine position is not conserved in fungal ACC, and no other phospho-dependent protein–protein interactions of fungal ACC have been described. INTRO | |
| 140 146 fungal taxonomy_domain The BRCA1-interacting phosphoserine position is not conserved in fungal ACC, and no other phospho-dependent protein–protein interactions of fungal ACC have been described. INTRO | |
| 147 150 ACC protein_type The BRCA1-interacting phosphoserine position is not conserved in fungal ACC, and no other phospho-dependent protein–protein interactions of fungal ACC have been described. INTRO | |
| 3 8 yeast taxonomy_domain In yeast ACC, phosphorylation sites have been identified at Ser2, Ser735, Ser1148, Ser1157 and Ser1162 (ref.). INTRO | |
| 9 12 ACC protein_type In yeast ACC, phosphorylation sites have been identified at Ser2, Ser735, Ser1148, Ser1157 and Ser1162 (ref.). INTRO | |
| 14 35 phosphorylation sites site In yeast ACC, phosphorylation sites have been identified at Ser2, Ser735, Ser1148, Ser1157 and Ser1162 (ref.). INTRO | |
| 60 64 Ser2 residue_name_number In yeast ACC, phosphorylation sites have been identified at Ser2, Ser735, Ser1148, Ser1157 and Ser1162 (ref.). INTRO | |
| 66 72 Ser735 residue_name_number In yeast ACC, phosphorylation sites have been identified at Ser2, Ser735, Ser1148, Ser1157 and Ser1162 (ref.). INTRO | |
| 74 81 Ser1148 residue_name_number In yeast ACC, phosphorylation sites have been identified at Ser2, Ser735, Ser1148, Ser1157 and Ser1162 (ref.). INTRO | |
| 83 90 Ser1157 residue_name_number In yeast ACC, phosphorylation sites have been identified at Ser2, Ser735, Ser1148, Ser1157 and Ser1162 (ref.). INTRO | |
| 95 102 Ser1162 residue_name_number In yeast ACC, phosphorylation sites have been identified at Ser2, Ser735, Ser1148, Ser1157 and Ser1162 (ref.). INTRO | |
| 15 22 Ser1157 residue_name_number Of these, only Ser1157 is highly conserved in fungal ACC and aligns to Ser1216 in human ACC1. INTRO | |
| 26 42 highly conserved protein_state Of these, only Ser1157 is highly conserved in fungal ACC and aligns to Ser1216 in human ACC1. INTRO | |
| 46 52 fungal taxonomy_domain Of these, only Ser1157 is highly conserved in fungal ACC and aligns to Ser1216 in human ACC1. INTRO | |
| 53 56 ACC protein_type Of these, only Ser1157 is highly conserved in fungal ACC and aligns to Ser1216 in human ACC1. INTRO | |
| 61 70 aligns to experimental_method Of these, only Ser1157 is highly conserved in fungal ACC and aligns to Ser1216 in human ACC1. INTRO | |
| 71 78 Ser1216 residue_name_number Of these, only Ser1157 is highly conserved in fungal ACC and aligns to Ser1216 in human ACC1. INTRO | |
| 82 87 human species Of these, only Ser1157 is highly conserved in fungal ACC and aligns to Ser1216 in human ACC1. INTRO | |
| 88 92 ACC1 protein Of these, only Ser1157 is highly conserved in fungal ACC and aligns to Ser1216 in human ACC1. INTRO | |
| 4 19 phosphorylation ptm Its phosphorylation by the AMPK homologue SNF1 results in strongly reduced ACC activity. INTRO | |
| 27 31 AMPK protein Its phosphorylation by the AMPK homologue SNF1 results in strongly reduced ACC activity. INTRO | |
| 42 46 SNF1 protein Its phosphorylation by the AMPK homologue SNF1 results in strongly reduced ACC activity. INTRO | |
| 75 78 ACC protein_type Its phosphorylation by the AMPK homologue SNF1 results in strongly reduced ACC activity. INTRO | |
| 37 40 ACC protein_type Despite the outstanding relevance of ACC in primary metabolism and disease, the dynamic organization and regulation of the giant eukaryotic, and in particular fungal ACC, remain poorly characterized. INTRO | |
| 129 139 eukaryotic taxonomy_domain Despite the outstanding relevance of ACC in primary metabolism and disease, the dynamic organization and regulation of the giant eukaryotic, and in particular fungal ACC, remain poorly characterized. INTRO | |
| 159 165 fungal taxonomy_domain Despite the outstanding relevance of ACC in primary metabolism and disease, the dynamic organization and regulation of the giant eukaryotic, and in particular fungal ACC, remain poorly characterized. INTRO | |
| 166 169 ACC protein_type Despite the outstanding relevance of ACC in primary metabolism and disease, the dynamic organization and regulation of the giant eukaryotic, and in particular fungal ACC, remain poorly characterized. INTRO | |
| 20 29 structure evidence Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 33 57 Saccharomyces cerevisiae species Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 59 62 Sce species Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 64 67 ACC protein_type Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 68 70 CD structure_element Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 105 115 structures evidence Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 119 124 human species Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 126 129 Hsa species Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 131 134 ACC protein_type Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 135 137 CD structure_element Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 142 158 larger fragments mutant Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 162 168 fungal taxonomy_domain Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 169 172 ACC protein_type Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 178 201 Chaetomium thermophilum species Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 203 206 Cth species Here we provide the structure of Saccharomyces cerevisiae (Sce) ACC CD, intermediate- and low-resolution structures of human (Hsa) ACC CD and larger fragments of fungal ACC from Chaetomium thermophilum (Cth; Fig. 1a). INTRO | |
| 28 56 small-angle X-ray scattering experimental_method Integrating these data with small-angle X-ray scattering (SAXS) and electron microscopy (EM) observations yield a comprehensive representation of the dynamic structure and regulation of fungal ACC. INTRO | |
| 58 62 SAXS experimental_method Integrating these data with small-angle X-ray scattering (SAXS) and electron microscopy (EM) observations yield a comprehensive representation of the dynamic structure and regulation of fungal ACC. INTRO | |
| 68 87 electron microscopy experimental_method Integrating these data with small-angle X-ray scattering (SAXS) and electron microscopy (EM) observations yield a comprehensive representation of the dynamic structure and regulation of fungal ACC. INTRO | |
| 89 91 EM experimental_method Integrating these data with small-angle X-ray scattering (SAXS) and electron microscopy (EM) observations yield a comprehensive representation of the dynamic structure and regulation of fungal ACC. INTRO | |
| 186 192 fungal taxonomy_domain Integrating these data with small-angle X-ray scattering (SAXS) and electron microscopy (EM) observations yield a comprehensive representation of the dynamic structure and regulation of fungal ACC. INTRO | |
| 193 196 ACC protein_type Integrating these data with small-angle X-ray scattering (SAXS) and electron microscopy (EM) observations yield a comprehensive representation of the dynamic structure and regulation of fungal ACC. INTRO | |
| 24 29 yeast taxonomy_domain The organization of the yeast ACC CD RESULTS | |
| 30 33 ACC protein_type The organization of the yeast ACC CD RESULTS | |
| 34 36 CD structure_element The organization of the yeast ACC CD RESULTS | |
| 21 44 structure determination experimental_method First, we focused on structure determination of the 82-kDa CD. RESULTS | |
| 59 61 CD structure_element First, we focused on structure determination of the 82-kDa CD. RESULTS | |
| 4 21 crystal structure evidence The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 29 31 CD structure_element The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 35 41 SceACC protein The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 43 46 Sce species The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 46 48 CD structure_element The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 88 108 experimental phasing experimental_method The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 113 120 refined experimental_method The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 124 129 Rwork evidence The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 130 135 Rfree evidence The crystal structure of the CD of SceACC (SceCD) was determined at 3.0 Å resolution by experimental phasing and refined to Rwork/Rfree=0.20/0.24 (Table 1). RESULTS | |
| 26 29 Sce species The overall extent of the SceCD is 70 by 75 Å (Fig. 1b and Supplementary Fig. 1a,b), and the attachment points of the N-terminal 26-residue linker to the BCCP domain and the C-terminal CT domain are separated by 46 Å (the N- and C termini are indicated with spheres in Fig. 1b). RESULTS | |
| 29 31 CD structure_element The overall extent of the SceCD is 70 by 75 Å (Fig. 1b and Supplementary Fig. 1a,b), and the attachment points of the N-terminal 26-residue linker to the BCCP domain and the C-terminal CT domain are separated by 46 Å (the N- and C termini are indicated with spheres in Fig. 1b). RESULTS | |
| 129 146 26-residue linker structure_element The overall extent of the SceCD is 70 by 75 Å (Fig. 1b and Supplementary Fig. 1a,b), and the attachment points of the N-terminal 26-residue linker to the BCCP domain and the C-terminal CT domain are separated by 46 Å (the N- and C termini are indicated with spheres in Fig. 1b). RESULTS | |
| 154 158 BCCP structure_element The overall extent of the SceCD is 70 by 75 Å (Fig. 1b and Supplementary Fig. 1a,b), and the attachment points of the N-terminal 26-residue linker to the BCCP domain and the C-terminal CT domain are separated by 46 Å (the N- and C termini are indicated with spheres in Fig. 1b). RESULTS | |
| 185 187 CT structure_element The overall extent of the SceCD is 70 by 75 Å (Fig. 1b and Supplementary Fig. 1a,b), and the attachment points of the N-terminal 26-residue linker to the BCCP domain and the C-terminal CT domain are separated by 46 Å (the N- and C termini are indicated with spheres in Fig. 1b). RESULTS | |
| 0 3 Sce species SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 3 5 CD structure_element SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 53 69 α-helical domain structure_element SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 71 74 CDN structure_element SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 91 122 four-helix bundle linker domain structure_element SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 124 127 CDL structure_element SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 146 173 α–β-fold C-terminal domains structure_element SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 175 179 CDC1 structure_element SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 180 184 CDC2 structure_element SceCD comprises four distinct domains, an N-terminal α-helical domain (CDN), and a central four-helix bundle linker domain (CDL), followed by two α–β-fold C-terminal domains (CDC1/CDC2). RESULTS | |
| 0 3 CDN structure_element CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 20 27 C shape protein_state CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 56 81 regular four-helix bundle structure_element CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 83 88 Nα3-6 structure_element CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 110 125 helical hairpin structure_element CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 127 132 Nα8,9 structure_element CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 142 157 bridging region structure_element CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 172 179 helices structure_element CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 181 194 Nα1,2,7,10–12 structure_element CDN adopts a letter C shape, where one of the ends is a regular four-helix bundle (Nα3-6), the other end is a helical hairpin (Nα8,9) and the bridging region comprises six helices (Nα1,2,7,10–12). RESULTS | |
| 0 3 CDL structure_element CDL is composed of a small, irregular four-helix bundle (Lα1–4) and tightly interacts with the open face of CDC1 via an interface of 1,300 Å2 involving helices Lα3 and Lα4. RESULTS | |
| 21 55 small, irregular four-helix bundle structure_element CDL is composed of a small, irregular four-helix bundle (Lα1–4) and tightly interacts with the open face of CDC1 via an interface of 1,300 Å2 involving helices Lα3 and Lα4. RESULTS | |
| 57 62 Lα1–4 structure_element CDL is composed of a small, irregular four-helix bundle (Lα1–4) and tightly interacts with the open face of CDC1 via an interface of 1,300 Å2 involving helices Lα3 and Lα4. RESULTS | |
| 108 112 CDC1 structure_element CDL is composed of a small, irregular four-helix bundle (Lα1–4) and tightly interacts with the open face of CDC1 via an interface of 1,300 Å2 involving helices Lα3 and Lα4. RESULTS | |
| 120 129 interface site CDL is composed of a small, irregular four-helix bundle (Lα1–4) and tightly interacts with the open face of CDC1 via an interface of 1,300 Å2 involving helices Lα3 and Lα4. RESULTS | |
| 152 159 helices structure_element CDL is composed of a small, irregular four-helix bundle (Lα1–4) and tightly interacts with the open face of CDC1 via an interface of 1,300 Å2 involving helices Lα3 and Lα4. RESULTS | |
| 160 163 Lα3 structure_element CDL is composed of a small, irregular four-helix bundle (Lα1–4) and tightly interacts with the open face of CDC1 via an interface of 1,300 Å2 involving helices Lα3 and Lα4. RESULTS | |
| 168 171 Lα4 structure_element CDL is composed of a small, irregular four-helix bundle (Lα1–4) and tightly interacts with the open face of CDC1 via an interface of 1,300 Å2 involving helices Lα3 and Lα4. RESULTS | |
| 0 3 CDL structure_element CDL does not interact with CDN apart from the covalent linkage and forms only a small contact to CDC2 via a loop between Lα2/α3 and the N-terminal end of Lα1, with an interface area of 400 Å2. RESULTS | |
| 27 30 CDN structure_element CDL does not interact with CDN apart from the covalent linkage and forms only a small contact to CDC2 via a loop between Lα2/α3 and the N-terminal end of Lα1, with an interface area of 400 Å2. RESULTS | |
| 97 101 CDC2 structure_element CDL does not interact with CDN apart from the covalent linkage and forms only a small contact to CDC2 via a loop between Lα2/α3 and the N-terminal end of Lα1, with an interface area of 400 Å2. RESULTS | |
| 108 112 loop structure_element CDL does not interact with CDN apart from the covalent linkage and forms only a small contact to CDC2 via a loop between Lα2/α3 and the N-terminal end of Lα1, with an interface area of 400 Å2. RESULTS | |
| 121 127 Lα2/α3 structure_element CDL does not interact with CDN apart from the covalent linkage and forms only a small contact to CDC2 via a loop between Lα2/α3 and the N-terminal end of Lα1, with an interface area of 400 Å2. RESULTS | |
| 154 157 Lα1 structure_element CDL does not interact with CDN apart from the covalent linkage and forms only a small contact to CDC2 via a loop between Lα2/α3 and the N-terminal end of Lα1, with an interface area of 400 Å2. RESULTS | |
| 167 176 interface site CDL does not interact with CDN apart from the covalent linkage and forms only a small contact to CDC2 via a loop between Lα2/α3 and the N-terminal end of Lα1, with an interface area of 400 Å2. RESULTS | |
| 0 4 CDC1 structure_element CDC1/CDC2 share a common fold; they are composed of six-stranded β-sheets flanked on one side by two long, bent helices inserted between strands β3/β4 and β4/β5. RESULTS | |
| 5 9 CDC2 structure_element CDC1/CDC2 share a common fold; they are composed of six-stranded β-sheets flanked on one side by two long, bent helices inserted between strands β3/β4 and β4/β5. RESULTS | |
| 52 73 six-stranded β-sheets structure_element CDC1/CDC2 share a common fold; they are composed of six-stranded β-sheets flanked on one side by two long, bent helices inserted between strands β3/β4 and β4/β5. RESULTS | |
| 101 119 long, bent helices structure_element CDC1/CDC2 share a common fold; they are composed of six-stranded β-sheets flanked on one side by two long, bent helices inserted between strands β3/β4 and β4/β5. RESULTS | |
| 137 144 strands structure_element CDC1/CDC2 share a common fold; they are composed of six-stranded β-sheets flanked on one side by two long, bent helices inserted between strands β3/β4 and β4/β5. RESULTS | |
| 145 150 β3/β4 structure_element CDC1/CDC2 share a common fold; they are composed of six-stranded β-sheets flanked on one side by two long, bent helices inserted between strands β3/β4 and β4/β5. RESULTS | |
| 155 160 β4/β5 structure_element CDC1/CDC2 share a common fold; they are composed of six-stranded β-sheets flanked on one side by two long, bent helices inserted between strands β3/β4 and β4/β5. RESULTS | |
| 0 4 CDC2 structure_element CDC2 is extended at its C terminus by an additional β-strand and an irregular β-hairpin. RESULTS | |
| 8 16 extended protein_state CDC2 is extended at its C terminus by an additional β-strand and an irregular β-hairpin. RESULTS | |
| 52 60 β-strand structure_element CDC2 is extended at its C terminus by an additional β-strand and an irregular β-hairpin. RESULTS | |
| 68 87 irregular β-hairpin structure_element CDC2 is extended at its C terminus by an additional β-strand and an irregular β-hairpin. RESULTS | |
| 18 44 root mean square deviation evidence On the basis of a root mean square deviation of main chain atom positions of 2.2 Å, CDC1/CDC2 are structurally more closely related to each other than to any other protein (Fig. 1c); they may thus have evolved by duplication. RESULTS | |
| 84 88 CDC1 structure_element On the basis of a root mean square deviation of main chain atom positions of 2.2 Å, CDC1/CDC2 are structurally more closely related to each other than to any other protein (Fig. 1c); they may thus have evolved by duplication. RESULTS | |
| 89 93 CDC2 structure_element On the basis of a root mean square deviation of main chain atom positions of 2.2 Å, CDC1/CDC2 are structurally more closely related to each other than to any other protein (Fig. 1c); they may thus have evolved by duplication. RESULTS | |
| 55 58 CDN structure_element Close structural homologues could not be found for the CDN or the CDC domains. RESULTS | |
| 66 69 CDC structure_element Close structural homologues could not be found for the CDN or the CDC domains. RESULTS | |
| 2 17 regulatory loop structure_element A regulatory loop mediates interdomain interactions RESULTS | |
| 34 55 insect-cell-expressed experimental_method To define the functional state of insect-cell-expressed ACC variants, we employed mass spectrometry (MS) for phosphorylation site detection. RESULTS | |
| 56 59 ACC protein_type To define the functional state of insect-cell-expressed ACC variants, we employed mass spectrometry (MS) for phosphorylation site detection. RESULTS | |
| 82 99 mass spectrometry experimental_method To define the functional state of insect-cell-expressed ACC variants, we employed mass spectrometry (MS) for phosphorylation site detection. RESULTS | |
| 101 103 MS experimental_method To define the functional state of insect-cell-expressed ACC variants, we employed mass spectrometry (MS) for phosphorylation site detection. RESULTS | |
| 109 139 phosphorylation site detection experimental_method To define the functional state of insect-cell-expressed ACC variants, we employed mass spectrometry (MS) for phosphorylation site detection. RESULTS | |
| 3 24 insect-cell-expressed experimental_method In insect-cell-expressed full-length SceACC, the highly conserved Ser1157 is the only fully occupied phosphorylation site with functional relevance in S. cerevisiae. RESULTS | |
| 25 36 full-length protein_state In insect-cell-expressed full-length SceACC, the highly conserved Ser1157 is the only fully occupied phosphorylation site with functional relevance in S. cerevisiae. RESULTS | |
| 37 43 SceACC protein In insect-cell-expressed full-length SceACC, the highly conserved Ser1157 is the only fully occupied phosphorylation site with functional relevance in S. cerevisiae. RESULTS | |
| 49 65 highly conserved protein_state In insect-cell-expressed full-length SceACC, the highly conserved Ser1157 is the only fully occupied phosphorylation site with functional relevance in S. cerevisiae. RESULTS | |
| 66 73 Ser1157 residue_name_number In insect-cell-expressed full-length SceACC, the highly conserved Ser1157 is the only fully occupied phosphorylation site with functional relevance in S. cerevisiae. RESULTS | |
| 86 100 fully occupied protein_state In insect-cell-expressed full-length SceACC, the highly conserved Ser1157 is the only fully occupied phosphorylation site with functional relevance in S. cerevisiae. RESULTS | |
| 101 121 phosphorylation site site In insect-cell-expressed full-length SceACC, the highly conserved Ser1157 is the only fully occupied phosphorylation site with functional relevance in S. cerevisiae. RESULTS | |
| 151 164 S. cerevisiae species In insect-cell-expressed full-length SceACC, the highly conserved Ser1157 is the only fully occupied phosphorylation site with functional relevance in S. cerevisiae. RESULTS | |
| 11 26 phosphorylation ptm Additional phosphorylation was detected for Ser2101 and Tyr2179; however, these sites are neither conserved across fungal ACC nor natively phosphorylated in yeast. RESULTS | |
| 44 51 Ser2101 residue_name_number Additional phosphorylation was detected for Ser2101 and Tyr2179; however, these sites are neither conserved across fungal ACC nor natively phosphorylated in yeast. RESULTS | |
| 56 63 Tyr2179 residue_name_number Additional phosphorylation was detected for Ser2101 and Tyr2179; however, these sites are neither conserved across fungal ACC nor natively phosphorylated in yeast. RESULTS | |
| 90 107 neither conserved protein_state Additional phosphorylation was detected for Ser2101 and Tyr2179; however, these sites are neither conserved across fungal ACC nor natively phosphorylated in yeast. RESULTS | |
| 115 121 fungal taxonomy_domain Additional phosphorylation was detected for Ser2101 and Tyr2179; however, these sites are neither conserved across fungal ACC nor natively phosphorylated in yeast. RESULTS | |
| 122 125 ACC protein_type Additional phosphorylation was detected for Ser2101 and Tyr2179; however, these sites are neither conserved across fungal ACC nor natively phosphorylated in yeast. RESULTS | |
| 126 153 nor natively phosphorylated protein_state Additional phosphorylation was detected for Ser2101 and Tyr2179; however, these sites are neither conserved across fungal ACC nor natively phosphorylated in yeast. RESULTS | |
| 157 162 yeast taxonomy_domain Additional phosphorylation was detected for Ser2101 and Tyr2179; however, these sites are neither conserved across fungal ACC nor natively phosphorylated in yeast. RESULTS | |
| 0 2 MS experimental_method MS analysis of dissolved crystals confirmed the phosphorylated state of Ser1157 also in SceCD crystals. RESULTS | |
| 15 33 dissolved crystals experimental_method MS analysis of dissolved crystals confirmed the phosphorylated state of Ser1157 also in SceCD crystals. RESULTS | |
| 48 62 phosphorylated protein_state MS analysis of dissolved crystals confirmed the phosphorylated state of Ser1157 also in SceCD crystals. RESULTS | |
| 72 79 Ser1157 residue_name_number MS analysis of dissolved crystals confirmed the phosphorylated state of Ser1157 also in SceCD crystals. RESULTS | |
| 88 91 Sce species MS analysis of dissolved crystals confirmed the phosphorylated state of Ser1157 also in SceCD crystals. RESULTS | |
| 91 93 CD structure_element MS analysis of dissolved crystals confirmed the phosphorylated state of Ser1157 also in SceCD crystals. RESULTS | |
| 94 102 crystals evidence MS analysis of dissolved crystals confirmed the phosphorylated state of Ser1157 also in SceCD crystals. RESULTS | |
| 4 7 Sce species The SceCD structure thus authentically represents the state of SceACC, where the enzyme is inhibited by SNF1-dependent phosphorylation. RESULTS | |
| 7 9 CD structure_element The SceCD structure thus authentically represents the state of SceACC, where the enzyme is inhibited by SNF1-dependent phosphorylation. RESULTS | |
| 10 19 structure evidence The SceCD structure thus authentically represents the state of SceACC, where the enzyme is inhibited by SNF1-dependent phosphorylation. RESULTS | |
| 63 69 SceACC protein The SceCD structure thus authentically represents the state of SceACC, where the enzyme is inhibited by SNF1-dependent phosphorylation. RESULTS | |
| 81 87 enzyme protein The SceCD structure thus authentically represents the state of SceACC, where the enzyme is inhibited by SNF1-dependent phosphorylation. RESULTS | |
| 91 100 inhibited protein_state The SceCD structure thus authentically represents the state of SceACC, where the enzyme is inhibited by SNF1-dependent phosphorylation. RESULTS | |
| 104 134 SNF1-dependent phosphorylation ptm The SceCD structure thus authentically represents the state of SceACC, where the enzyme is inhibited by SNF1-dependent phosphorylation. RESULTS | |
| 7 10 Sce species In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 10 12 CD structure_element In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 13 30 crystal structure evidence In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 36 50 phosphorylated protein_state In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 51 58 Ser1157 residue_name_number In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 72 101 regulatory 36-amino-acid loop structure_element In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 110 117 strands structure_element In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 118 120 β2 structure_element In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 125 127 β3 structure_element In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 131 135 CDC1 structure_element In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 179 193 less-conserved protein_state In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 194 215 phosphorylation sites site In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 217 224 Ser1148 residue_name_number In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 229 236 Ser1162 residue_name_number In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 251 256 yeast taxonomy_domain In the SceCD crystal structure, the phosphorylated Ser1157 resides in a regulatory 36-amino-acid loop between strands β2 and β3 of CDC1 (Fig. 1b,d), which contains two additional less-conserved phosphorylation sites (Ser1148 and Ser1162) confirmed in yeast, but not occupied here. RESULTS | |
| 5 20 regulatory loop structure_element This regulatory loop wedges between the CDC1 and CDC2 domains and provides the largest contribution to the interdomain interface. RESULTS | |
| 40 44 CDC1 structure_element This regulatory loop wedges between the CDC1 and CDC2 domains and provides the largest contribution to the interdomain interface. RESULTS | |
| 49 53 CDC2 structure_element This regulatory loop wedges between the CDC1 and CDC2 domains and provides the largest contribution to the interdomain interface. RESULTS | |
| 107 128 interdomain interface site This regulatory loop wedges between the CDC1 and CDC2 domains and provides the largest contribution to the interdomain interface. RESULTS | |
| 29 44 regulatory loop structure_element The N-terminal region of the regulatory loop also directly contacts the C-terminal region of CDC2 leading into CT. RESULTS | |
| 93 97 CDC2 structure_element The N-terminal region of the regulatory loop also directly contacts the C-terminal region of CDC2 leading into CT. RESULTS | |
| 111 113 CT structure_element The N-terminal region of the regulatory loop also directly contacts the C-terminal region of CDC2 leading into CT. RESULTS | |
| 0 18 Phosphoserine 1157 residue_name_number Phosphoserine 1157 is tightly bound by two highly conserved arginines (Arg1173 and Arg1260) of CDC1 (Fig. 1d). RESULTS | |
| 43 59 highly conserved protein_state Phosphoserine 1157 is tightly bound by two highly conserved arginines (Arg1173 and Arg1260) of CDC1 (Fig. 1d). RESULTS | |
| 60 69 arginines residue_name Phosphoserine 1157 is tightly bound by two highly conserved arginines (Arg1173 and Arg1260) of CDC1 (Fig. 1d). RESULTS | |
| 71 78 Arg1173 residue_name_number Phosphoserine 1157 is tightly bound by two highly conserved arginines (Arg1173 and Arg1260) of CDC1 (Fig. 1d). RESULTS | |
| 83 90 Arg1260 residue_name_number Phosphoserine 1157 is tightly bound by two highly conserved arginines (Arg1173 and Arg1260) of CDC1 (Fig. 1d). RESULTS | |
| 95 99 CDC1 structure_element Phosphoserine 1157 is tightly bound by two highly conserved arginines (Arg1173 and Arg1260) of CDC1 (Fig. 1d). RESULTS | |
| 23 37 phosphorylated protein_state Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 38 45 Ser1157 residue_name_number Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 72 87 regulatory loop structure_element Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 116 137 phosphorylation sites site Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 138 145 Ser1148 residue_name_number Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 150 157 Ser1162 residue_name_number Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 165 174 same loop structure_element Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 236 251 regulatory loop structure_element Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 260 264 CDC1 structure_element Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 269 273 CDC2 structure_element Already the binding of phosphorylated Ser1157 apparently stabilizes the regulatory loop conformation; the accessory phosphorylation sites Ser1148 and Ser1162 in the same loop may further modulate the strength of interaction between the regulatory loop and the CDC1 and CDC2 domains. RESULTS | |
| 0 15 Phosphorylation ptm Phosphorylation of the regulatory loop thus determines interdomain interactions of CDC1 and CDC2, suggesting that it may exert its regulatory function by modifying the overall structure and dynamics of the CD. RESULTS | |
| 23 38 regulatory loop structure_element Phosphorylation of the regulatory loop thus determines interdomain interactions of CDC1 and CDC2, suggesting that it may exert its regulatory function by modifying the overall structure and dynamics of the CD. RESULTS | |
| 83 87 CDC1 structure_element Phosphorylation of the regulatory loop thus determines interdomain interactions of CDC1 and CDC2, suggesting that it may exert its regulatory function by modifying the overall structure and dynamics of the CD. RESULTS | |
| 92 96 CDC2 structure_element Phosphorylation of the regulatory loop thus determines interdomain interactions of CDC1 and CDC2, suggesting that it may exert its regulatory function by modifying the overall structure and dynamics of the CD. RESULTS | |
| 206 208 CD structure_element Phosphorylation of the regulatory loop thus determines interdomain interactions of CDC1 and CDC2, suggesting that it may exert its regulatory function by modifying the overall structure and dynamics of the CD. RESULTS | |
| 23 30 Ser1157 residue_name_number The functional role of Ser1157 was confirmed by an activity assay based on the incorporation of radioactive carbonate into acid non-volatile material. RESULTS | |
| 51 65 activity assay experimental_method The functional role of Ser1157 was confirmed by an activity assay based on the incorporation of radioactive carbonate into acid non-volatile material. RESULTS | |
| 0 14 Phosphorylated protein_state Phosphorylated SceACC shows only residual activity (kcat=0.4±0.2 s−1, s.d. based on five replicate measurements), which increases 16-fold (kcat=6.5±0.3 s−1) after dephosphorylation with λ protein phosphatase. RESULTS | |
| 15 21 SceACC protein Phosphorylated SceACC shows only residual activity (kcat=0.4±0.2 s−1, s.d. based on five replicate measurements), which increases 16-fold (kcat=6.5±0.3 s−1) after dephosphorylation with λ protein phosphatase. RESULTS | |
| 52 56 kcat evidence Phosphorylated SceACC shows only residual activity (kcat=0.4±0.2 s−1, s.d. based on five replicate measurements), which increases 16-fold (kcat=6.5±0.3 s−1) after dephosphorylation with λ protein phosphatase. RESULTS | |
| 139 143 kcat evidence Phosphorylated SceACC shows only residual activity (kcat=0.4±0.2 s−1, s.d. based on five replicate measurements), which increases 16-fold (kcat=6.5±0.3 s−1) after dephosphorylation with λ protein phosphatase. RESULTS | |
| 186 207 λ protein phosphatase protein_type Phosphorylated SceACC shows only residual activity (kcat=0.4±0.2 s−1, s.d. based on five replicate measurements), which increases 16-fold (kcat=6.5±0.3 s−1) after dephosphorylation with λ protein phosphatase. RESULTS | |
| 24 40 dephosphorylated protein_state The values obtained for dephosphorylated SceACC are comparable to earlier measurements of non-phosphorylated yeast ACC expressed in E. coli. RESULTS | |
| 41 47 SceACC protein The values obtained for dephosphorylated SceACC are comparable to earlier measurements of non-phosphorylated yeast ACC expressed in E. coli. RESULTS | |
| 90 108 non-phosphorylated protein_state The values obtained for dephosphorylated SceACC are comparable to earlier measurements of non-phosphorylated yeast ACC expressed in E. coli. RESULTS | |
| 109 114 yeast taxonomy_domain The values obtained for dephosphorylated SceACC are comparable to earlier measurements of non-phosphorylated yeast ACC expressed in E. coli. RESULTS | |
| 115 118 ACC protein_type The values obtained for dephosphorylated SceACC are comparable to earlier measurements of non-phosphorylated yeast ACC expressed in E. coli. RESULTS | |
| 119 131 expressed in experimental_method The values obtained for dephosphorylated SceACC are comparable to earlier measurements of non-phosphorylated yeast ACC expressed in E. coli. RESULTS | |
| 132 139 E. coli species The values obtained for dephosphorylated SceACC are comparable to earlier measurements of non-phosphorylated yeast ACC expressed in E. coli. RESULTS | |
| 13 15 CD structure_element The variable CD is conserved between yeast and human RESULTS | |
| 19 28 conserved protein_state The variable CD is conserved between yeast and human RESULTS | |
| 37 42 yeast taxonomy_domain The variable CD is conserved between yeast and human RESULTS | |
| 47 52 human species The variable CD is conserved between yeast and human RESULTS | |
| 31 37 fungal taxonomy_domain To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 42 47 human species To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 48 51 ACC protein_type To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 52 54 CD structure_element To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 59 83 determined the structure experimental_method To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 89 94 human species To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 95 108 ACC1 fragment mutant To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 128 130 BT structure_element To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 135 137 CD structure_element To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 147 155 HsaBT-CD mutant To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 162 167 lacks protein_state To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 179 183 BCCP structure_element To compare the organization of fungal and human ACC CD, we determined the structure of a human ACC1 fragment that comprises the BT and CD domains (HsaBT-CD), but lacks the mobile BCCP in between (Fig. 1a). RESULTS | |
| 3 28 experimentally phased map evidence An experimentally phased map was obtained at 3.7 Å resolution for a cadmium-derivatized crystal and was interpreted by a poly-alanine model (Fig. 1e and Table 1). RESULTS | |
| 68 75 cadmium chemical An experimentally phased map was obtained at 3.7 Å resolution for a cadmium-derivatized crystal and was interpreted by a poly-alanine model (Fig. 1e and Table 1). RESULTS | |
| 17 19 CD structure_element Each of the four CD domains in HsaBT-CD individually resembles the corresponding SceCD domain; however, human and yeast CDs exhibit distinct overall structures. RESULTS | |
| 31 39 HsaBT-CD mutant Each of the four CD domains in HsaBT-CD individually resembles the corresponding SceCD domain; however, human and yeast CDs exhibit distinct overall structures. RESULTS | |
| 81 84 Sce species Each of the four CD domains in HsaBT-CD individually resembles the corresponding SceCD domain; however, human and yeast CDs exhibit distinct overall structures. RESULTS | |
| 84 86 CD structure_element Each of the four CD domains in HsaBT-CD individually resembles the corresponding SceCD domain; however, human and yeast CDs exhibit distinct overall structures. RESULTS | |
| 104 109 human species Each of the four CD domains in HsaBT-CD individually resembles the corresponding SceCD domain; however, human and yeast CDs exhibit distinct overall structures. RESULTS | |
| 114 119 yeast taxonomy_domain Each of the four CD domains in HsaBT-CD individually resembles the corresponding SceCD domain; however, human and yeast CDs exhibit distinct overall structures. RESULTS | |
| 120 123 CDs structure_element Each of the four CD domains in HsaBT-CD individually resembles the corresponding SceCD domain; however, human and yeast CDs exhibit distinct overall structures. RESULTS | |
| 149 159 structures evidence Each of the four CD domains in HsaBT-CD individually resembles the corresponding SceCD domain; however, human and yeast CDs exhibit distinct overall structures. RESULTS | |
| 45 48 Sce species In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 48 50 CD structure_element In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 88 91 CDL structure_element In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 96 100 CDC1 structure_element In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 117 125 HsaBT-CD mutant In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 135 140 human species In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 141 144 CDL structure_element In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 145 149 CDC1 structure_element In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 187 200 superposition experimental_method In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 204 209 human species In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 214 219 yeast taxonomy_domain In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 220 224 CDC2 structure_element In agreement with their tight interaction in SceCD, the relative spatial arrangement of CDL and CDC1 is preserved in HsaBT-CD, but the human CDL/CDC1 didomain is tilted by 30° based on a superposition of human and yeast CDC2 (Supplementary Fig. 1c). RESULTS | |
| 31 34 CDL structure_element As a result, the N terminus of CDL at helix Lα1, which connects to CDN, is shifted by 12 Å. Remarkably, CDN of HsaBT-CD adopts a completely different orientation compared with SceCD. RESULTS | |
| 38 43 helix structure_element As a result, the N terminus of CDL at helix Lα1, which connects to CDN, is shifted by 12 Å. Remarkably, CDN of HsaBT-CD adopts a completely different orientation compared with SceCD. RESULTS | |
| 44 47 Lα1 structure_element As a result, the N terminus of CDL at helix Lα1, which connects to CDN, is shifted by 12 Å. Remarkably, CDN of HsaBT-CD adopts a completely different orientation compared with SceCD. RESULTS | |
| 67 70 CDN structure_element As a result, the N terminus of CDL at helix Lα1, which connects to CDN, is shifted by 12 Å. Remarkably, CDN of HsaBT-CD adopts a completely different orientation compared with SceCD. RESULTS | |
| 104 107 CDN structure_element As a result, the N terminus of CDL at helix Lα1, which connects to CDN, is shifted by 12 Å. Remarkably, CDN of HsaBT-CD adopts a completely different orientation compared with SceCD. RESULTS | |
| 111 119 HsaBT-CD mutant As a result, the N terminus of CDL at helix Lα1, which connects to CDN, is shifted by 12 Å. Remarkably, CDN of HsaBT-CD adopts a completely different orientation compared with SceCD. RESULTS | |
| 176 179 Sce species As a result, the N terminus of CDL at helix Lα1, which connects to CDN, is shifted by 12 Å. Remarkably, CDN of HsaBT-CD adopts a completely different orientation compared with SceCD. RESULTS | |
| 179 181 CD structure_element As a result, the N terminus of CDL at helix Lα1, which connects to CDN, is shifted by 12 Å. Remarkably, CDN of HsaBT-CD adopts a completely different orientation compared with SceCD. RESULTS | |
| 5 8 CDL structure_element With CDL/CDC1 superposed, CDN in HsaBT-CD is rotated by 160° around a hinge at the connection of CDN/CDL (Supplementary Fig. 1d). RESULTS | |
| 9 13 CDC1 structure_element With CDL/CDC1 superposed, CDN in HsaBT-CD is rotated by 160° around a hinge at the connection of CDN/CDL (Supplementary Fig. 1d). RESULTS | |
| 14 24 superposed experimental_method With CDL/CDC1 superposed, CDN in HsaBT-CD is rotated by 160° around a hinge at the connection of CDN/CDL (Supplementary Fig. 1d). RESULTS | |
| 26 29 CDN structure_element With CDL/CDC1 superposed, CDN in HsaBT-CD is rotated by 160° around a hinge at the connection of CDN/CDL (Supplementary Fig. 1d). RESULTS | |
| 33 41 HsaBT-CD mutant With CDL/CDC1 superposed, CDN in HsaBT-CD is rotated by 160° around a hinge at the connection of CDN/CDL (Supplementary Fig. 1d). RESULTS | |
| 70 75 hinge structure_element With CDL/CDC1 superposed, CDN in HsaBT-CD is rotated by 160° around a hinge at the connection of CDN/CDL (Supplementary Fig. 1d). RESULTS | |
| 97 100 CDN structure_element With CDL/CDC1 superposed, CDN in HsaBT-CD is rotated by 160° around a hinge at the connection of CDN/CDL (Supplementary Fig. 1d). RESULTS | |
| 101 104 CDL structure_element With CDL/CDC1 superposed, CDN in HsaBT-CD is rotated by 160° around a hinge at the connection of CDN/CDL (Supplementary Fig. 1d). RESULTS | |
| 42 45 CDN structure_element This rotation displaces the N terminus of CDN in HsaBT-CD by 51 Å compared with SceCD, resulting in a separation of the attachment points of the N-terminal linker to the BCCP domain and the C-terminal CT domain by 67 Å (the attachment points are indicated with spheres in Fig. 1e). RESULTS | |
| 49 57 HsaBT-CD mutant This rotation displaces the N terminus of CDN in HsaBT-CD by 51 Å compared with SceCD, resulting in a separation of the attachment points of the N-terminal linker to the BCCP domain and the C-terminal CT domain by 67 Å (the attachment points are indicated with spheres in Fig. 1e). RESULTS | |
| 80 83 Sce species This rotation displaces the N terminus of CDN in HsaBT-CD by 51 Å compared with SceCD, resulting in a separation of the attachment points of the N-terminal linker to the BCCP domain and the C-terminal CT domain by 67 Å (the attachment points are indicated with spheres in Fig. 1e). RESULTS | |
| 83 85 CD structure_element This rotation displaces the N terminus of CDN in HsaBT-CD by 51 Å compared with SceCD, resulting in a separation of the attachment points of the N-terminal linker to the BCCP domain and the C-terminal CT domain by 67 Å (the attachment points are indicated with spheres in Fig. 1e). RESULTS | |
| 156 162 linker structure_element This rotation displaces the N terminus of CDN in HsaBT-CD by 51 Å compared with SceCD, resulting in a separation of the attachment points of the N-terminal linker to the BCCP domain and the C-terminal CT domain by 67 Å (the attachment points are indicated with spheres in Fig. 1e). RESULTS | |
| 170 181 BCCP domain structure_element This rotation displaces the N terminus of CDN in HsaBT-CD by 51 Å compared with SceCD, resulting in a separation of the attachment points of the N-terminal linker to the BCCP domain and the C-terminal CT domain by 67 Å (the attachment points are indicated with spheres in Fig. 1e). RESULTS | |
| 201 203 CT structure_element This rotation displaces the N terminus of CDN in HsaBT-CD by 51 Å compared with SceCD, resulting in a separation of the attachment points of the N-terminal linker to the BCCP domain and the C-terminal CT domain by 67 Å (the attachment points are indicated with spheres in Fig. 1e). RESULTS | |
| 4 6 BT structure_element The BT domain of HsaBT-CD consists of a helix that is surrounded at its N terminus by an antiparallel eight-stranded β-barrel. RESULTS | |
| 17 25 HsaBT-CD mutant The BT domain of HsaBT-CD consists of a helix that is surrounded at its N terminus by an antiparallel eight-stranded β-barrel. RESULTS | |
| 40 45 helix structure_element The BT domain of HsaBT-CD consists of a helix that is surrounded at its N terminus by an antiparallel eight-stranded β-barrel. RESULTS | |
| 89 125 antiparallel eight-stranded β-barrel structure_element The BT domain of HsaBT-CD consists of a helix that is surrounded at its N terminus by an antiparallel eight-stranded β-barrel. RESULTS | |
| 17 19 BT structure_element It resembles the BT of propionyl-CoA carboxylase; only the four C-terminal strands of the β-barrel are slightly tilted. RESULTS | |
| 23 48 propionyl-CoA carboxylase protein_type It resembles the BT of propionyl-CoA carboxylase; only the four C-terminal strands of the β-barrel are slightly tilted. RESULTS | |
| 75 98 strands of the β-barrel structure_element It resembles the BT of propionyl-CoA carboxylase; only the four C-terminal strands of the β-barrel are slightly tilted. RESULTS | |
| 16 18 MS experimental_method On the basis of MS analysis of insect-cell-expressed human full-length ACC, Ser80 shows the highest degree of phosphorylation (90%). RESULTS | |
| 31 52 insect-cell-expressed experimental_method On the basis of MS analysis of insect-cell-expressed human full-length ACC, Ser80 shows the highest degree of phosphorylation (90%). RESULTS | |
| 53 58 human species On the basis of MS analysis of insect-cell-expressed human full-length ACC, Ser80 shows the highest degree of phosphorylation (90%). RESULTS | |
| 59 70 full-length protein_state On the basis of MS analysis of insect-cell-expressed human full-length ACC, Ser80 shows the highest degree of phosphorylation (90%). RESULTS | |
| 71 74 ACC protein_type On the basis of MS analysis of insect-cell-expressed human full-length ACC, Ser80 shows the highest degree of phosphorylation (90%). RESULTS | |
| 76 81 Ser80 residue_name_number On the basis of MS analysis of insect-cell-expressed human full-length ACC, Ser80 shows the highest degree of phosphorylation (90%). RESULTS | |
| 110 125 phosphorylation ptm On the basis of MS analysis of insect-cell-expressed human full-length ACC, Ser80 shows the highest degree of phosphorylation (90%). RESULTS | |
| 0 5 Ser29 residue_name_number Ser29 and Ser1263, implicated in insulin-dependent phosphorylation and BRCA1 binding, respectively, are phosphorylated at intermediate levels (40%). RESULTS | |
| 10 17 Ser1263 residue_name_number Ser29 and Ser1263, implicated in insulin-dependent phosphorylation and BRCA1 binding, respectively, are phosphorylated at intermediate levels (40%). RESULTS | |
| 33 66 insulin-dependent phosphorylation ptm Ser29 and Ser1263, implicated in insulin-dependent phosphorylation and BRCA1 binding, respectively, are phosphorylated at intermediate levels (40%). RESULTS | |
| 71 76 BRCA1 protein Ser29 and Ser1263, implicated in insulin-dependent phosphorylation and BRCA1 binding, respectively, are phosphorylated at intermediate levels (40%). RESULTS | |
| 104 118 phosphorylated protein_state Ser29 and Ser1263, implicated in insulin-dependent phosphorylation and BRCA1 binding, respectively, are phosphorylated at intermediate levels (40%). RESULTS | |
| 4 20 highly conserved protein_state The highly conserved Ser1216 (corresponding to S. cerevisiae Ser1157), as well as Ser1201, both in the regulatory loop discussed above, are not phosphorylated. RESULTS | |
| 21 28 Ser1216 residue_name_number The highly conserved Ser1216 (corresponding to S. cerevisiae Ser1157), as well as Ser1201, both in the regulatory loop discussed above, are not phosphorylated. RESULTS | |
| 47 60 S. cerevisiae species The highly conserved Ser1216 (corresponding to S. cerevisiae Ser1157), as well as Ser1201, both in the regulatory loop discussed above, are not phosphorylated. RESULTS | |
| 61 68 Ser1157 residue_name_number The highly conserved Ser1216 (corresponding to S. cerevisiae Ser1157), as well as Ser1201, both in the regulatory loop discussed above, are not phosphorylated. RESULTS | |
| 82 89 Ser1201 residue_name_number The highly conserved Ser1216 (corresponding to S. cerevisiae Ser1157), as well as Ser1201, both in the regulatory loop discussed above, are not phosphorylated. RESULTS | |
| 103 118 regulatory loop structure_element The highly conserved Ser1216 (corresponding to S. cerevisiae Ser1157), as well as Ser1201, both in the regulatory loop discussed above, are not phosphorylated. RESULTS | |
| 140 158 not phosphorylated protein_state The highly conserved Ser1216 (corresponding to S. cerevisiae Ser1157), as well as Ser1201, both in the regulatory loop discussed above, are not phosphorylated. RESULTS | |
| 18 33 phosphorylation ptm However, residual phosphorylation levels were detected for Ser1204 (7%) and Ser1218 (7%) in the same loop. RESULTS | |
| 59 66 Ser1204 residue_name_number However, residual phosphorylation levels were detected for Ser1204 (7%) and Ser1218 (7%) in the same loop. RESULTS | |
| 76 83 Ser1218 residue_name_number However, residual phosphorylation levels were detected for Ser1204 (7%) and Ser1218 (7%) in the same loop. RESULTS | |
| 96 105 same loop structure_element However, residual phosphorylation levels were detected for Ser1204 (7%) and Ser1218 (7%) in the same loop. RESULTS | |
| 0 2 MS experimental_method MS analysis of the HsaBT-CD crystallization sample reveals partial proteolytic digestion of the regulatory loop. RESULTS | |
| 19 27 HsaBT-CD mutant MS analysis of the HsaBT-CD crystallization sample reveals partial proteolytic digestion of the regulatory loop. RESULTS | |
| 28 50 crystallization sample evidence MS analysis of the HsaBT-CD crystallization sample reveals partial proteolytic digestion of the regulatory loop. RESULTS | |
| 96 111 regulatory loop structure_element MS analysis of the HsaBT-CD crystallization sample reveals partial proteolytic digestion of the regulatory loop. RESULTS | |
| 21 30 this loop structure_element Accordingly, most of this loop is not represented in the HsaBT-CD crystal structure. RESULTS | |
| 57 65 HsaBT-CD mutant Accordingly, most of this loop is not represented in the HsaBT-CD crystal structure. RESULTS | |
| 66 83 crystal structure evidence Accordingly, most of this loop is not represented in the HsaBT-CD crystal structure. RESULTS | |
| 4 14 absence of protein_state The absence of the regulatory loop might be linked to the less-restrained interface of CDL/CDC1 and CDC2 and altered relative orientations of these domains. RESULTS | |
| 19 34 regulatory loop structure_element The absence of the regulatory loop might be linked to the less-restrained interface of CDL/CDC1 and CDC2 and altered relative orientations of these domains. RESULTS | |
| 58 73 less-restrained protein_state The absence of the regulatory loop might be linked to the less-restrained interface of CDL/CDC1 and CDC2 and altered relative orientations of these domains. RESULTS | |
| 74 83 interface site The absence of the regulatory loop might be linked to the less-restrained interface of CDL/CDC1 and CDC2 and altered relative orientations of these domains. RESULTS | |
| 87 90 CDL structure_element The absence of the regulatory loop might be linked to the less-restrained interface of CDL/CDC1 and CDC2 and altered relative orientations of these domains. RESULTS | |
| 91 95 CDC1 structure_element The absence of the regulatory loop might be linked to the less-restrained interface of CDL/CDC1 and CDC2 and altered relative orientations of these domains. RESULTS | |
| 100 104 CDC2 structure_element The absence of the regulatory loop might be linked to the less-restrained interface of CDL/CDC1 and CDC2 and altered relative orientations of these domains. RESULTS | |
| 148 155 domains structure_element The absence of the regulatory loop might be linked to the less-restrained interface of CDL/CDC1 and CDC2 and altered relative orientations of these domains. RESULTS | |
| 12 27 regulatory loop structure_element Besides the regulatory loop, also the phosphopeptide target region for BRCA1 interaction is not resolved presumably because of pronounced flexibility. RESULTS | |
| 38 66 phosphopeptide target region site Besides the regulatory loop, also the phosphopeptide target region for BRCA1 interaction is not resolved presumably because of pronounced flexibility. RESULTS | |
| 71 76 BRCA1 protein Besides the regulatory loop, also the phosphopeptide target region for BRCA1 interaction is not resolved presumably because of pronounced flexibility. RESULTS | |
| 16 24 isolated experimental_method At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 25 30 yeast taxonomy_domain At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 35 40 human species At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 41 43 CD structure_element At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 49 68 structural analysis experimental_method At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 108 114 hinges structure_element At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 156 174 CDN/CDL connection structure_element At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 216 219 CDL structure_element At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 220 224 CDC1 structure_element At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 229 233 CDC2 structure_element At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 257 272 phosphorylation ptm At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 280 295 regulatory loop structure_element At the level of isolated yeast and human CD, the structural analysis indicates the presence of at least two hinges, one with large-scale flexibility at the CDN/CDL connection, and one with tunable plasticity between CDL/CDC1 and CDC2, plausibly affected by phosphorylation in the regulatory loop region. RESULTS | |
| 19 21 CD structure_element The integration of CD into the fungal ACC multienzyme RESULTS | |
| 31 37 fungal taxonomy_domain The integration of CD into the fungal ACC multienzyme RESULTS | |
| 38 53 ACC multienzyme protein_type The integration of CD into the fungal ACC multienzyme RESULTS | |
| 63 69 fungal taxonomy_domain To further obtain insights into the functional architecture of fungal ACC, we characterized larger multidomain fragments up to the intact enzymes. RESULTS | |
| 70 73 ACC protein_type To further obtain insights into the functional architecture of fungal ACC, we characterized larger multidomain fragments up to the intact enzymes. RESULTS | |
| 92 120 larger multidomain fragments mutant To further obtain insights into the functional architecture of fungal ACC, we characterized larger multidomain fragments up to the intact enzymes. RESULTS | |
| 131 137 intact protein_state To further obtain insights into the functional architecture of fungal ACC, we characterized larger multidomain fragments up to the intact enzymes. RESULTS | |
| 138 145 enzymes protein To further obtain insights into the functional architecture of fungal ACC, we characterized larger multidomain fragments up to the intact enzymes. RESULTS | |
| 6 27 molecular replacement experimental_method Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 37 43 fungal taxonomy_domain Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 44 47 ACC protein_type Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 48 50 CD structure_element Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 55 57 CT structure_element Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 78 88 structures evidence Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 94 101 variant mutant Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 113 116 Cth species Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 116 118 CT structure_element Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 123 127 CDC1 structure_element Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 128 132 CDC2 structure_element Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 136 153 two crystal forms evidence Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 187 202 CthCD-CTCter1/2 mutant Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 235 238 Cth species Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 238 240 CT structure_element Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 262 264 CD structure_element Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 286 294 CthCD-CT mutant Using molecular replacement based on fungal ACC CD and CT models, we obtained structures of a variant comprising CthCT and CDC1/CDC2 in two crystal forms at resolutions of 3.6 and 4.5 Å (CthCD-CTCter1/2), respectively, as well as of a CthCT linked to the entire CD at 7.2 Å resolution (CthCD-CT; Figs 1a and 2, Table 1). RESULTS | |
| 67 97 larger BC-containing fragments mutant No crystals diffracting to sufficient resolution were obtained for larger BC-containing fragments, or for full-length Cth or SceACC. RESULTS | |
| 106 117 full-length protein_state No crystals diffracting to sufficient resolution were obtained for larger BC-containing fragments, or for full-length Cth or SceACC. RESULTS | |
| 118 121 Cth species No crystals diffracting to sufficient resolution were obtained for larger BC-containing fragments, or for full-length Cth or SceACC. RESULTS | |
| 125 131 SceACC protein No crystals diffracting to sufficient resolution were obtained for larger BC-containing fragments, or for full-length Cth or SceACC. RESULTS | |
| 3 28 improve crystallizability experimental_method To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). RESULTS | |
| 33 42 generated experimental_method To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). RESULTS | |
| 43 57 ΔBCCP variants mutant To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). RESULTS | |
| 61 72 full-length protein_state To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). RESULTS | |
| 73 76 ACC protein_type To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). RESULTS | |
| 94 107 SAXS analysis experimental_method To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). RESULTS | |
| 132 138 intact protein_state To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). RESULTS | |
| 139 142 ACC protein_type To improve crystallizability, we generated ΔBCCP variants of full-length ACC, which, based on SAXS analysis, preserve properties of intact ACC (Supplementary Table 1 and Supplementary Fig. 2a–c). RESULTS | |
| 4 12 CthΔBCCP mutant For CthΔBCCP, crystals diffracting to 8.4 Å resolution were obtained. RESULTS | |
| 14 22 crystals evidence For CthΔBCCP, crystals diffracting to 8.4 Å resolution were obtained. RESULTS | |
| 9 30 molecular replacement experimental_method However, molecular replacement did not reveal a unique positioning of the BC domain. RESULTS | |
| 74 76 BC structure_element However, molecular replacement did not reveal a unique positioning of the BC domain. RESULTS | |
| 50 60 structures evidence Owing to the limited resolution the discussion of structures of CthCD-CT and CthΔBCCP is restricted to the analysis of domain localization. RESULTS | |
| 64 72 CthCD-CT mutant Owing to the limited resolution the discussion of structures of CthCD-CT and CthΔBCCP is restricted to the analysis of domain localization. RESULTS | |
| 77 85 CthΔBCCP mutant Owing to the limited resolution the discussion of structures of CthCD-CT and CthΔBCCP is restricted to the analysis of domain localization. RESULTS | |
| 7 23 these structures evidence Still, these structures contribute considerably to the visualization of an intrinsically dynamic fungal ACC. RESULTS | |
| 89 96 dynamic protein_state Still, these structures contribute considerably to the visualization of an intrinsically dynamic fungal ACC. RESULTS | |
| 97 103 fungal taxonomy_domain Still, these structures contribute considerably to the visualization of an intrinsically dynamic fungal ACC. RESULTS | |
| 104 107 ACC protein_type Still, these structures contribute considerably to the visualization of an intrinsically dynamic fungal ACC. RESULTS | |
| 13 31 crystal structures evidence In all these crystal structures, the CT domains build a canonical head-to-tail dimer, with active sites formed by contributions from both protomers (Fig. 2 and Supplementary Fig. 3a). RESULTS | |
| 37 39 CT structure_element In all these crystal structures, the CT domains build a canonical head-to-tail dimer, with active sites formed by contributions from both protomers (Fig. 2 and Supplementary Fig. 3a). RESULTS | |
| 66 78 head-to-tail protein_state In all these crystal structures, the CT domains build a canonical head-to-tail dimer, with active sites formed by contributions from both protomers (Fig. 2 and Supplementary Fig. 3a). RESULTS | |
| 79 84 dimer oligomeric_state In all these crystal structures, the CT domains build a canonical head-to-tail dimer, with active sites formed by contributions from both protomers (Fig. 2 and Supplementary Fig. 3a). RESULTS | |
| 91 103 active sites site In all these crystal structures, the CT domains build a canonical head-to-tail dimer, with active sites formed by contributions from both protomers (Fig. 2 and Supplementary Fig. 3a). RESULTS | |
| 138 147 protomers oligomeric_state In all these crystal structures, the CT domains build a canonical head-to-tail dimer, with active sites formed by contributions from both protomers (Fig. 2 and Supplementary Fig. 3a). RESULTS | |
| 4 14 connection structure_element The connection of CD and CT is provided by a 10-residue peptide stretch, which links the N terminus of CT to the irregular β-hairpin/β-strand extension of CDC2 (Supplementary Fig. 3b). RESULTS | |
| 18 20 CD structure_element The connection of CD and CT is provided by a 10-residue peptide stretch, which links the N terminus of CT to the irregular β-hairpin/β-strand extension of CDC2 (Supplementary Fig. 3b). RESULTS | |
| 25 27 CT structure_element The connection of CD and CT is provided by a 10-residue peptide stretch, which links the N terminus of CT to the irregular β-hairpin/β-strand extension of CDC2 (Supplementary Fig. 3b). RESULTS | |
| 45 71 10-residue peptide stretch residue_range The connection of CD and CT is provided by a 10-residue peptide stretch, which links the N terminus of CT to the irregular β-hairpin/β-strand extension of CDC2 (Supplementary Fig. 3b). RESULTS | |
| 103 105 CT structure_element The connection of CD and CT is provided by a 10-residue peptide stretch, which links the N terminus of CT to the irregular β-hairpin/β-strand extension of CDC2 (Supplementary Fig. 3b). RESULTS | |
| 113 151 irregular β-hairpin/β-strand extension structure_element The connection of CD and CT is provided by a 10-residue peptide stretch, which links the N terminus of CT to the irregular β-hairpin/β-strand extension of CDC2 (Supplementary Fig. 3b). RESULTS | |
| 155 159 CDC2 structure_element The connection of CD and CT is provided by a 10-residue peptide stretch, which links the N terminus of CT to the irregular β-hairpin/β-strand extension of CDC2 (Supplementary Fig. 3b). RESULTS | |
| 4 21 connecting region structure_element The connecting region is remarkably similar in isolated CD and CthCD-CTCter structures, indicating inherent conformational stability. RESULTS | |
| 47 55 isolated protein_state The connecting region is remarkably similar in isolated CD and CthCD-CTCter structures, indicating inherent conformational stability. RESULTS | |
| 56 58 CD structure_element The connecting region is remarkably similar in isolated CD and CthCD-CTCter structures, indicating inherent conformational stability. RESULTS | |
| 63 75 CthCD-CTCter mutant The connecting region is remarkably similar in isolated CD and CthCD-CTCter structures, indicating inherent conformational stability. RESULTS | |
| 76 86 structures evidence The connecting region is remarkably similar in isolated CD and CthCD-CTCter structures, indicating inherent conformational stability. RESULTS | |
| 0 2 CD structure_element CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 3 5 CT structure_element CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 90 109 β-hairpin extension structure_element CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 113 117 CDC2 structure_element CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 133 137 loop structure_element CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 146 159 strands β2/β3 structure_element CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 167 176 CT N-lobe structure_element CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 195 204 conserved protein_state CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 205 217 RxxGxN motif structure_element CD/CT contacts are only formed in direct vicinity of the covalent linkage and involve the β-hairpin extension of CDC2 as well as the loop between strands β2/β3 of the CT N-lobe, which contains a conserved RxxGxN motif. RESULTS | |
| 17 21 loop structure_element The neighbouring loop on the CT side (between CT β1/β2) is displaced by 2.5 Å compared to isolated CT structures (Supplementary Fig. 3c). RESULTS | |
| 29 31 CT structure_element The neighbouring loop on the CT side (between CT β1/β2) is displaced by 2.5 Å compared to isolated CT structures (Supplementary Fig. 3c). RESULTS | |
| 46 48 CT structure_element The neighbouring loop on the CT side (between CT β1/β2) is displaced by 2.5 Å compared to isolated CT structures (Supplementary Fig. 3c). RESULTS | |
| 49 51 β1 structure_element The neighbouring loop on the CT side (between CT β1/β2) is displaced by 2.5 Å compared to isolated CT structures (Supplementary Fig. 3c). RESULTS | |
| 52 54 β2 structure_element The neighbouring loop on the CT side (between CT β1/β2) is displaced by 2.5 Å compared to isolated CT structures (Supplementary Fig. 3c). RESULTS | |
| 90 98 isolated protein_state The neighbouring loop on the CT side (between CT β1/β2) is displaced by 2.5 Å compared to isolated CT structures (Supplementary Fig. 3c). RESULTS | |
| 99 101 CT structure_element The neighbouring loop on the CT side (between CT β1/β2) is displaced by 2.5 Å compared to isolated CT structures (Supplementary Fig. 3c). RESULTS | |
| 102 112 structures evidence The neighbouring loop on the CT side (between CT β1/β2) is displaced by 2.5 Å compared to isolated CT structures (Supplementary Fig. 3c). RESULTS | |
| 98 107 interface site On the basis of an interface area of ∼600 Å2 and its edge-to-edge connection characteristics, the interface between CT and CD might be classified as conformationally variable. RESULTS | |
| 116 118 CT structure_element On the basis of an interface area of ∼600 Å2 and its edge-to-edge connection characteristics, the interface between CT and CD might be classified as conformationally variable. RESULTS | |
| 123 125 CD structure_element On the basis of an interface area of ∼600 Å2 and its edge-to-edge connection characteristics, the interface between CT and CD might be classified as conformationally variable. RESULTS | |
| 87 89 CD structure_element Indeed, the comparison of the positioning of eight instances of the C-terminal part of CD relative to CT in crystal structures determined here, reveals flexible interdomain linking (Fig. 3a). RESULTS | |
| 102 104 CT structure_element Indeed, the comparison of the positioning of eight instances of the C-terminal part of CD relative to CT in crystal structures determined here, reveals flexible interdomain linking (Fig. 3a). RESULTS | |
| 108 126 crystal structures evidence Indeed, the comparison of the positioning of eight instances of the C-terminal part of CD relative to CT in crystal structures determined here, reveals flexible interdomain linking (Fig. 3a). RESULTS | |
| 127 137 determined experimental_method Indeed, the comparison of the positioning of eight instances of the C-terminal part of CD relative to CT in crystal structures determined here, reveals flexible interdomain linking (Fig. 3a). RESULTS | |
| 4 21 CDC2/CT interface site The CDC2/CT interface acts as a true hinge with observed rotation up to 16°, which results in a translocation of the distal end of CDC2 by 8 Å. RESULTS | |
| 32 42 true hinge structure_element The CDC2/CT interface acts as a true hinge with observed rotation up to 16°, which results in a translocation of the distal end of CDC2 by 8 Å. RESULTS | |
| 131 135 CDC2 structure_element The CDC2/CT interface acts as a true hinge with observed rotation up to 16°, which results in a translocation of the distal end of CDC2 by 8 Å. RESULTS | |
| 4 13 interface site The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 22 26 CDC2 structure_element The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 31 34 CDL structure_element The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 35 39 CDC1 structure_element The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 66 80 phosphorylated protein_state The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 81 96 regulatory loop structure_element The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 104 107 Sce species The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 107 109 CD structure_element The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 110 119 structure evidence The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 147 161 CD–CT junction structure_element The interface between CDC2 and CDL/CDC1, which is mediated by the phosphorylated regulatory loop in the SceCD structure, is less variable than the CD–CT junction, and permits only limited rotation and tilting (Fig. 3b). RESULTS | |
| 26 41 phosphorylation ptm Analysis of the impact of phosphorylation on the interface between CDC2 and CDL/CDC1 in CthACC variant structures is precluded by the limited crystallographic resolution. RESULTS | |
| 49 58 interface site Analysis of the impact of phosphorylation on the interface between CDC2 and CDL/CDC1 in CthACC variant structures is precluded by the limited crystallographic resolution. RESULTS | |
| 67 71 CDC2 structure_element Analysis of the impact of phosphorylation on the interface between CDC2 and CDL/CDC1 in CthACC variant structures is precluded by the limited crystallographic resolution. RESULTS | |
| 76 79 CDL structure_element Analysis of the impact of phosphorylation on the interface between CDC2 and CDL/CDC1 in CthACC variant structures is precluded by the limited crystallographic resolution. RESULTS | |
| 80 84 CDC1 structure_element Analysis of the impact of phosphorylation on the interface between CDC2 and CDL/CDC1 in CthACC variant structures is precluded by the limited crystallographic resolution. RESULTS | |
| 88 102 CthACC variant mutant Analysis of the impact of phosphorylation on the interface between CDC2 and CDL/CDC1 in CthACC variant structures is precluded by the limited crystallographic resolution. RESULTS | |
| 103 113 structures evidence Analysis of the impact of phosphorylation on the interface between CDC2 and CDL/CDC1 in CthACC variant structures is precluded by the limited crystallographic resolution. RESULTS | |
| 9 11 MS experimental_method However, MS analysis of CthCD-CT and CthΔBCCP constructs revealed between 60 and 70% phosphorylation of Ser1170 (corresponding to SceACC Ser1157). RESULTS | |
| 24 32 CthCD-CT mutant However, MS analysis of CthCD-CT and CthΔBCCP constructs revealed between 60 and 70% phosphorylation of Ser1170 (corresponding to SceACC Ser1157). RESULTS | |
| 37 45 CthΔBCCP mutant However, MS analysis of CthCD-CT and CthΔBCCP constructs revealed between 60 and 70% phosphorylation of Ser1170 (corresponding to SceACC Ser1157). RESULTS | |
| 85 100 phosphorylation ptm However, MS analysis of CthCD-CT and CthΔBCCP constructs revealed between 60 and 70% phosphorylation of Ser1170 (corresponding to SceACC Ser1157). RESULTS | |
| 104 111 Ser1170 residue_name_number However, MS analysis of CthCD-CT and CthΔBCCP constructs revealed between 60 and 70% phosphorylation of Ser1170 (corresponding to SceACC Ser1157). RESULTS | |
| 130 136 SceACC protein However, MS analysis of CthCD-CT and CthΔBCCP constructs revealed between 60 and 70% phosphorylation of Ser1170 (corresponding to SceACC Ser1157). RESULTS | |
| 137 144 Ser1157 residue_name_number However, MS analysis of CthCD-CT and CthΔBCCP constructs revealed between 60 and 70% phosphorylation of Ser1170 (corresponding to SceACC Ser1157). RESULTS | |
| 4 7 CDN structure_element The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 39 42 CDL structure_element The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 43 47 CDC1 structure_element The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 112 122 structures evidence The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 126 129 Sce species The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 129 131 CD structure_element The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 140 163 larger CthACC fragments mutant The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 165 168 CDN structure_element The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 257 266 protomers oligomeric_state The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 270 278 CthCD-CT mutant The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 287 295 protomer oligomeric_state The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 299 307 CthΔBCCP mutant The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 320 331 CthCD-CT1/2 mutant The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 336 345 CthΔBCCP1 mutant The CDN domain positioning relative to CDL/CDC1 is highly variable with three main orientations observed in the structures of SceCD and the larger CthACC fragments: CDN tilts, resulting in a displacement of its N terminus by 23 Å (Fig. 4a, observed in both protomers of CthCD-CT and one protomer of CthΔBCCP, denoted as CthCD-CT1/2 and CthΔBCCP1, respectively). RESULTS | |
| 13 16 CDN structure_element In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 35 41 hinges structure_element In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 68 71 CDN structure_element In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 72 75 CDL structure_element In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 116 124 protomer oligomeric_state In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 128 136 CthΔBCCP mutant In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 149 158 CthΔBCCP2 mutant In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 191 194 Sce species In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 194 196 CD structure_element In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 229 240 anchor site site In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 249 260 BCCP linker structure_element In addition, CDN can rotate around hinges in the connection between CDN/CDL by 70° (Fig. 4b, observed in the second protomer of CthΔBCCP, denoted as CthΔBCCP2) and 160° (Fig. 4c, observed in SceCD) leading to displacement of the anchor site for the BCCP linker by up to 33 and 40 Å, respectively. RESULTS | |
| 34 36 CD structure_element Conformational variability in the CD thus contributes considerably to variations in the spacing between the BC and CT domains, and may extend to distance variations beyond the mobility range of the flexibly tethered BCCP. RESULTS | |
| 108 110 BC structure_element Conformational variability in the CD thus contributes considerably to variations in the spacing between the BC and CT domains, and may extend to distance variations beyond the mobility range of the flexibly tethered BCCP. RESULTS | |
| 115 117 CT structure_element Conformational variability in the CD thus contributes considerably to variations in the spacing between the BC and CT domains, and may extend to distance variations beyond the mobility range of the flexibly tethered BCCP. RESULTS | |
| 198 215 flexibly tethered protein_state Conformational variability in the CD thus contributes considerably to variations in the spacing between the BC and CT domains, and may extend to distance variations beyond the mobility range of the flexibly tethered BCCP. RESULTS | |
| 216 220 BCCP structure_element Conformational variability in the CD thus contributes considerably to variations in the spacing between the BC and CT domains, and may extend to distance variations beyond the mobility range of the flexibly tethered BCCP. RESULTS | |
| 73 79 fungal taxonomy_domain On the basis of the occurrence of related conformational changes between fungal and human ACC fragments, the observed set of conformations may well represent general states present in all eukaryotic ACCs. RESULTS | |
| 84 89 human species On the basis of the occurrence of related conformational changes between fungal and human ACC fragments, the observed set of conformations may well represent general states present in all eukaryotic ACCs. RESULTS | |
| 90 103 ACC fragments mutant On the basis of the occurrence of related conformational changes between fungal and human ACC fragments, the observed set of conformations may well represent general states present in all eukaryotic ACCs. RESULTS | |
| 188 198 eukaryotic taxonomy_domain On the basis of the occurrence of related conformational changes between fungal and human ACC fragments, the observed set of conformations may well represent general states present in all eukaryotic ACCs. RESULTS | |
| 199 203 ACCs protein_type On the basis of the occurrence of related conformational changes between fungal and human ACC fragments, the observed set of conformations may well represent general states present in all eukaryotic ACCs. RESULTS | |
| 42 48 fungal taxonomy_domain Large-scale conformational variability of fungal ACC RESULTS | |
| 49 52 ACC protein_type Large-scale conformational variability of fungal ACC RESULTS | |
| 34 40 fungal taxonomy_domain To obtain a comprehensive view of fungal ACC dynamics in solution, we employed SAXS and EM. RESULTS | |
| 41 44 ACC protein_type To obtain a comprehensive view of fungal ACC dynamics in solution, we employed SAXS and EM. RESULTS | |
| 54 65 in solution protein_state To obtain a comprehensive view of fungal ACC dynamics in solution, we employed SAXS and EM. RESULTS | |
| 79 83 SAXS experimental_method To obtain a comprehensive view of fungal ACC dynamics in solution, we employed SAXS and EM. RESULTS | |
| 88 90 EM experimental_method To obtain a comprehensive view of fungal ACC dynamics in solution, we employed SAXS and EM. RESULTS | |
| 0 4 SAXS experimental_method SAXS analysis of CthACC agrees with a dimeric state and an elongated shape with a maximum extent of 350 Å (Supplementary Table 1). RESULTS | |
| 17 23 CthACC protein SAXS analysis of CthACC agrees with a dimeric state and an elongated shape with a maximum extent of 350 Å (Supplementary Table 1). RESULTS | |
| 38 45 dimeric oligomeric_state SAXS analysis of CthACC agrees with a dimeric state and an elongated shape with a maximum extent of 350 Å (Supplementary Table 1). RESULTS | |
| 59 74 elongated shape protein_state SAXS analysis of CthACC agrees with a dimeric state and an elongated shape with a maximum extent of 350 Å (Supplementary Table 1). RESULTS | |
| 25 42 scattering curves evidence The smooth appearance of scattering curves and derived distance distributions might indicate substantial interdomain flexibility (Supplementary Fig. 2a–c). RESULTS | |
| 47 77 derived distance distributions evidence The smooth appearance of scattering curves and derived distance distributions might indicate substantial interdomain flexibility (Supplementary Fig. 2a–c). RESULTS | |
| 33 44 full-length protein_state Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 45 51 CthACC protein Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 52 61 particles evidence Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 76 78 MS experimental_method Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 106 120 phosphorylated protein_state Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 121 139 low-activity state protein_state Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 144 161 negative stain EM experimental_method Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 204 221 rod-like extended protein_state Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 225 233 U-shaped protein_state Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 234 243 particles evidence Direct observation of individual full-length CthACC particles, according to MS results predominantly in a phosphorylated low-activity state, in negative stain EM reveals a large set of conformations from rod-like extended to U-shaped particles. RESULTS | |
| 0 14 Class averages evidence Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 28 88 maximum-likelihood-based two-dimensional (2D) classification experimental_method Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 109 116 dimeric oligomeric_state Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 117 119 CT structure_element Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 135 139 full protein_state Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 140 150 BC–BCCP–CD mutant Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 170 178 protomer oligomeric_state Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 230 232 BC structure_element Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 233 235 CD structure_element Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 260 262 CT structure_element Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 263 268 dimer oligomeric_state Class averages, obtained by maximum-likelihood-based two-dimensional (2D) classification, are focused on the dimeric CT domain and the full BC–BCCP–CD domain of only one protomer, due to the non-coordinated motions of the lateral BC/CD regions relative to the CT dimer. RESULTS | |
| 38 41 CDN structure_element They identify the connections between CDN/CDL and between CDC2/CT as major contributors to conformational heterogeneity (Supplementary Fig. 4a,b). RESULTS | |
| 42 45 CDL structure_element They identify the connections between CDN/CDL and between CDC2/CT as major contributors to conformational heterogeneity (Supplementary Fig. 4a,b). RESULTS | |
| 58 62 CDC2 structure_element They identify the connections between CDN/CDL and between CDC2/CT as major contributors to conformational heterogeneity (Supplementary Fig. 4a,b). RESULTS | |
| 63 65 CT structure_element They identify the connections between CDN/CDL and between CDC2/CT as major contributors to conformational heterogeneity (Supplementary Fig. 4a,b). RESULTS | |
| 23 36 CDC2/CT hinge structure_element The flexibility in the CDC2/CT hinge appears substantially larger than the variations observed in the set of crystal structures. RESULTS | |
| 109 127 crystal structures evidence The flexibility in the CDC2/CT hinge appears substantially larger than the variations observed in the set of crystal structures. RESULTS | |
| 4 6 BC structure_element The BC domain is not completely disordered, but laterally attached to BT/CDN in a generally conserved position, albeit with increased flexibility. RESULTS | |
| 70 72 BT structure_element The BC domain is not completely disordered, but laterally attached to BT/CDN in a generally conserved position, albeit with increased flexibility. RESULTS | |
| 73 76 CDN structure_element The BC domain is not completely disordered, but laterally attached to BT/CDN in a generally conserved position, albeit with increased flexibility. RESULTS | |
| 82 110 generally conserved position protein_state The BC domain is not completely disordered, but laterally attached to BT/CDN in a generally conserved position, albeit with increased flexibility. RESULTS | |
| 26 59 linear and U-shaped conformations protein_state Surprisingly, in both the linear and U-shaped conformations, the approximate distances between the BC and CT active sites would remain larger than 110 Å. These observed distances are considerably larger than in static structures of any other related biotin-dependent carboxylase. RESULTS | |
| 99 101 BC structure_element Surprisingly, in both the linear and U-shaped conformations, the approximate distances between the BC and CT active sites would remain larger than 110 Å. These observed distances are considerably larger than in static structures of any other related biotin-dependent carboxylase. RESULTS | |
| 106 108 CT structure_element Surprisingly, in both the linear and U-shaped conformations, the approximate distances between the BC and CT active sites would remain larger than 110 Å. These observed distances are considerably larger than in static structures of any other related biotin-dependent carboxylase. RESULTS | |
| 109 121 active sites site Surprisingly, in both the linear and U-shaped conformations, the approximate distances between the BC and CT active sites would remain larger than 110 Å. These observed distances are considerably larger than in static structures of any other related biotin-dependent carboxylase. RESULTS | |
| 211 217 static protein_state Surprisingly, in both the linear and U-shaped conformations, the approximate distances between the BC and CT active sites would remain larger than 110 Å. These observed distances are considerably larger than in static structures of any other related biotin-dependent carboxylase. RESULTS | |
| 218 228 structures evidence Surprisingly, in both the linear and U-shaped conformations, the approximate distances between the BC and CT active sites would remain larger than 110 Å. These observed distances are considerably larger than in static structures of any other related biotin-dependent carboxylase. RESULTS | |
| 250 278 biotin-dependent carboxylase protein_type Surprisingly, in both the linear and U-shaped conformations, the approximate distances between the BC and CT active sites would remain larger than 110 Å. These observed distances are considerably larger than in static structures of any other related biotin-dependent carboxylase. RESULTS | |
| 47 61 BCCP–CD linker structure_element Furthermore, based on an average length of the BCCP–CD linker in fungal ACC of 26 amino acids, mobility of the BCCP alone would not be sufficient to bridge the active sites of BC and CT. RESULTS | |
| 65 71 fungal taxonomy_domain Furthermore, based on an average length of the BCCP–CD linker in fungal ACC of 26 amino acids, mobility of the BCCP alone would not be sufficient to bridge the active sites of BC and CT. RESULTS | |
| 72 75 ACC protein_type Furthermore, based on an average length of the BCCP–CD linker in fungal ACC of 26 amino acids, mobility of the BCCP alone would not be sufficient to bridge the active sites of BC and CT. RESULTS | |
| 79 93 26 amino acids residue_range Furthermore, based on an average length of the BCCP–CD linker in fungal ACC of 26 amino acids, mobility of the BCCP alone would not be sufficient to bridge the active sites of BC and CT. RESULTS | |
| 111 115 BCCP structure_element Furthermore, based on an average length of the BCCP–CD linker in fungal ACC of 26 amino acids, mobility of the BCCP alone would not be sufficient to bridge the active sites of BC and CT. RESULTS | |
| 160 172 active sites site Furthermore, based on an average length of the BCCP–CD linker in fungal ACC of 26 amino acids, mobility of the BCCP alone would not be sufficient to bridge the active sites of BC and CT. RESULTS | |
| 176 178 BC structure_element Furthermore, based on an average length of the BCCP–CD linker in fungal ACC of 26 amino acids, mobility of the BCCP alone would not be sufficient to bridge the active sites of BC and CT. RESULTS | |
| 183 185 CT structure_element Furthermore, based on an average length of the BCCP–CD linker in fungal ACC of 26 amino acids, mobility of the BCCP alone would not be sufficient to bridge the active sites of BC and CT. RESULTS | |
| 130 149 CDC1/CDC2 interface site The most relevant candidate site for mediating such additional flexibility and permitting an extended set of conformations is the CDC1/CDC2 interface, which is rigidified by the Ser1157-phosphorylated regulatory loop, as depicted in the SceCD crystal structure. RESULTS | |
| 178 185 Ser1157 residue_name_number The most relevant candidate site for mediating such additional flexibility and permitting an extended set of conformations is the CDC1/CDC2 interface, which is rigidified by the Ser1157-phosphorylated regulatory loop, as depicted in the SceCD crystal structure. RESULTS | |
| 186 200 phosphorylated protein_state The most relevant candidate site for mediating such additional flexibility and permitting an extended set of conformations is the CDC1/CDC2 interface, which is rigidified by the Ser1157-phosphorylated regulatory loop, as depicted in the SceCD crystal structure. RESULTS | |
| 201 216 regulatory loop structure_element The most relevant candidate site for mediating such additional flexibility and permitting an extended set of conformations is the CDC1/CDC2 interface, which is rigidified by the Ser1157-phosphorylated regulatory loop, as depicted in the SceCD crystal structure. RESULTS | |
| 237 240 Sce species The most relevant candidate site for mediating such additional flexibility and permitting an extended set of conformations is the CDC1/CDC2 interface, which is rigidified by the Ser1157-phosphorylated regulatory loop, as depicted in the SceCD crystal structure. RESULTS | |
| 240 242 CD structure_element The most relevant candidate site for mediating such additional flexibility and permitting an extended set of conformations is the CDC1/CDC2 interface, which is rigidified by the Ser1157-phosphorylated regulatory loop, as depicted in the SceCD crystal structure. RESULTS | |
| 243 260 crystal structure evidence The most relevant candidate site for mediating such additional flexibility and permitting an extended set of conformations is the CDC1/CDC2 interface, which is rigidified by the Ser1157-phosphorylated regulatory loop, as depicted in the SceCD crystal structure. RESULTS | |
| 32 38 fungal taxonomy_domain Altogether, the architecture of fungal ACC is based on the central dimeric CT domain (Fig. 4d). DISCUSS | |
| 39 42 ACC protein_type Altogether, the architecture of fungal ACC is based on the central dimeric CT domain (Fig. 4d). DISCUSS | |
| 67 74 dimeric oligomeric_state Altogether, the architecture of fungal ACC is based on the central dimeric CT domain (Fig. 4d). DISCUSS | |
| 75 77 CT structure_element Altogether, the architecture of fungal ACC is based on the central dimeric CT domain (Fig. 4d). DISCUSS | |
| 4 6 CD structure_element The CD consists of four distinct subdomains and acts as a tether from the CT to the mobile BCCP and an oriented BC domain. DISCUSS | |
| 33 43 subdomains structure_element The CD consists of four distinct subdomains and acts as a tether from the CT to the mobile BCCP and an oriented BC domain. DISCUSS | |
| 74 76 CT structure_element The CD consists of four distinct subdomains and acts as a tether from the CT to the mobile BCCP and an oriented BC domain. DISCUSS | |
| 84 90 mobile protein_state The CD consists of four distinct subdomains and acts as a tether from the CT to the mobile BCCP and an oriented BC domain. DISCUSS | |
| 91 95 BCCP structure_element The CD consists of four distinct subdomains and acts as a tether from the CT to the mobile BCCP and an oriented BC domain. DISCUSS | |
| 103 111 oriented protein_state The CD consists of four distinct subdomains and acts as a tether from the CT to the mobile BCCP and an oriented BC domain. DISCUSS | |
| 112 114 BC structure_element The CD consists of four distinct subdomains and acts as a tether from the CT to the mobile BCCP and an oriented BC domain. DISCUSS | |
| 4 6 CD structure_element The CD has no direct role in substrate recognition or catalysis but contributes to the regulation of all eukaryotic ACCs. DISCUSS | |
| 105 115 eukaryotic taxonomy_domain The CD has no direct role in substrate recognition or catalysis but contributes to the regulation of all eukaryotic ACCs. DISCUSS | |
| 116 120 ACCs protein_type The CD has no direct role in substrate recognition or catalysis but contributes to the regulation of all eukaryotic ACCs. DISCUSS | |
| 3 20 higher eukaryotic taxonomy_domain In higher eukaryotic ACCs, regulation via phosphorylation is achieved by combining the effects of phosphorylation at Ser80, Ser1201 and Ser1263. DISCUSS | |
| 21 25 ACCs protein_type In higher eukaryotic ACCs, regulation via phosphorylation is achieved by combining the effects of phosphorylation at Ser80, Ser1201 and Ser1263. DISCUSS | |
| 42 57 phosphorylation ptm In higher eukaryotic ACCs, regulation via phosphorylation is achieved by combining the effects of phosphorylation at Ser80, Ser1201 and Ser1263. DISCUSS | |
| 98 113 phosphorylation ptm In higher eukaryotic ACCs, regulation via phosphorylation is achieved by combining the effects of phosphorylation at Ser80, Ser1201 and Ser1263. DISCUSS | |
| 117 122 Ser80 residue_name_number In higher eukaryotic ACCs, regulation via phosphorylation is achieved by combining the effects of phosphorylation at Ser80, Ser1201 and Ser1263. DISCUSS | |
| 124 131 Ser1201 residue_name_number In higher eukaryotic ACCs, regulation via phosphorylation is achieved by combining the effects of phosphorylation at Ser80, Ser1201 and Ser1263. DISCUSS | |
| 136 143 Ser1263 residue_name_number In higher eukaryotic ACCs, regulation via phosphorylation is achieved by combining the effects of phosphorylation at Ser80, Ser1201 and Ser1263. DISCUSS | |
| 3 9 fungal taxonomy_domain In fungal ACC, however, Ser1157 in the regulatory loop of the CD is the only phosphorylation site that has been demonstrated to be both phosphorylated in vivo and involved in the regulation of ACC activity. DISCUSS | |
| 10 13 ACC protein_type In fungal ACC, however, Ser1157 in the regulatory loop of the CD is the only phosphorylation site that has been demonstrated to be both phosphorylated in vivo and involved in the regulation of ACC activity. DISCUSS | |
| 24 31 Ser1157 residue_name_number In fungal ACC, however, Ser1157 in the regulatory loop of the CD is the only phosphorylation site that has been demonstrated to be both phosphorylated in vivo and involved in the regulation of ACC activity. DISCUSS | |
| 39 54 regulatory loop structure_element In fungal ACC, however, Ser1157 in the regulatory loop of the CD is the only phosphorylation site that has been demonstrated to be both phosphorylated in vivo and involved in the regulation of ACC activity. DISCUSS | |
| 62 64 CD structure_element In fungal ACC, however, Ser1157 in the regulatory loop of the CD is the only phosphorylation site that has been demonstrated to be both phosphorylated in vivo and involved in the regulation of ACC activity. DISCUSS | |
| 77 97 phosphorylation site site In fungal ACC, however, Ser1157 in the regulatory loop of the CD is the only phosphorylation site that has been demonstrated to be both phosphorylated in vivo and involved in the regulation of ACC activity. DISCUSS | |
| 136 150 phosphorylated protein_state In fungal ACC, however, Ser1157 in the regulatory loop of the CD is the only phosphorylation site that has been demonstrated to be both phosphorylated in vivo and involved in the regulation of ACC activity. DISCUSS | |
| 193 196 ACC protein_type In fungal ACC, however, Ser1157 in the regulatory loop of the CD is the only phosphorylation site that has been demonstrated to be both phosphorylated in vivo and involved in the regulation of ACC activity. DISCUSS | |
| 7 21 phosphorylated protein_state In its phosphorylated state, the regulatory loop containing Ser1157 wedges between CDC1/CDC2 and presumably limits the conformational freedom at this interdomain interface. DISCUSS | |
| 33 48 regulatory loop structure_element In its phosphorylated state, the regulatory loop containing Ser1157 wedges between CDC1/CDC2 and presumably limits the conformational freedom at this interdomain interface. DISCUSS | |
| 60 67 Ser1157 residue_name_number In its phosphorylated state, the regulatory loop containing Ser1157 wedges between CDC1/CDC2 and presumably limits the conformational freedom at this interdomain interface. DISCUSS | |
| 83 87 CDC1 structure_element In its phosphorylated state, the regulatory loop containing Ser1157 wedges between CDC1/CDC2 and presumably limits the conformational freedom at this interdomain interface. DISCUSS | |
| 88 92 CDC2 structure_element In its phosphorylated state, the regulatory loop containing Ser1157 wedges between CDC1/CDC2 and presumably limits the conformational freedom at this interdomain interface. DISCUSS | |
| 119 141 conformational freedom protein_state In its phosphorylated state, the regulatory loop containing Ser1157 wedges between CDC1/CDC2 and presumably limits the conformational freedom at this interdomain interface. DISCUSS | |
| 150 171 interdomain interface site In its phosphorylated state, the regulatory loop containing Ser1157 wedges between CDC1/CDC2 and presumably limits the conformational freedom at this interdomain interface. DISCUSS | |
| 29 34 hinge structure_element However, flexibility at this hinge may be required for full ACC activity, as the distances between the BCCP anchor points and the active sites of BC and CT observed here are such large that mobility of the BCCP alone is not sufficient for substrate transfer. DISCUSS | |
| 55 72 full ACC activity protein_state However, flexibility at this hinge may be required for full ACC activity, as the distances between the BCCP anchor points and the active sites of BC and CT observed here are such large that mobility of the BCCP alone is not sufficient for substrate transfer. DISCUSS | |
| 103 121 BCCP anchor points structure_element However, flexibility at this hinge may be required for full ACC activity, as the distances between the BCCP anchor points and the active sites of BC and CT observed here are such large that mobility of the BCCP alone is not sufficient for substrate transfer. DISCUSS | |
| 130 142 active sites site However, flexibility at this hinge may be required for full ACC activity, as the distances between the BCCP anchor points and the active sites of BC and CT observed here are such large that mobility of the BCCP alone is not sufficient for substrate transfer. DISCUSS | |
| 146 148 BC structure_element However, flexibility at this hinge may be required for full ACC activity, as the distances between the BCCP anchor points and the active sites of BC and CT observed here are such large that mobility of the BCCP alone is not sufficient for substrate transfer. DISCUSS | |
| 153 155 CT structure_element However, flexibility at this hinge may be required for full ACC activity, as the distances between the BCCP anchor points and the active sites of BC and CT observed here are such large that mobility of the BCCP alone is not sufficient for substrate transfer. DISCUSS | |
| 206 210 BCCP structure_element However, flexibility at this hinge may be required for full ACC activity, as the distances between the BCCP anchor points and the active sites of BC and CT observed here are such large that mobility of the BCCP alone is not sufficient for substrate transfer. DISCUSS | |
| 49 55 fungal taxonomy_domain The current data thus suggest that regulation of fungal ACC is mediated by controlling the dynamics of the unique CD, rather than directly affecting catalytic turnover at the active sites of BC and CT. DISCUSS | |
| 56 59 ACC protein_type The current data thus suggest that regulation of fungal ACC is mediated by controlling the dynamics of the unique CD, rather than directly affecting catalytic turnover at the active sites of BC and CT. DISCUSS | |
| 107 113 unique protein_state The current data thus suggest that regulation of fungal ACC is mediated by controlling the dynamics of the unique CD, rather than directly affecting catalytic turnover at the active sites of BC and CT. DISCUSS | |
| 114 116 CD structure_element The current data thus suggest that regulation of fungal ACC is mediated by controlling the dynamics of the unique CD, rather than directly affecting catalytic turnover at the active sites of BC and CT. DISCUSS | |
| 175 187 active sites site The current data thus suggest that regulation of fungal ACC is mediated by controlling the dynamics of the unique CD, rather than directly affecting catalytic turnover at the active sites of BC and CT. DISCUSS | |
| 191 193 BC structure_element The current data thus suggest that regulation of fungal ACC is mediated by controlling the dynamics of the unique CD, rather than directly affecting catalytic turnover at the active sites of BC and CT. DISCUSS | |
| 198 200 CT structure_element The current data thus suggest that regulation of fungal ACC is mediated by controlling the dynamics of the unique CD, rather than directly affecting catalytic turnover at the active sites of BC and CT. DISCUSS | |
| 21 27 fungal taxonomy_domain A comparison between fungal and human ACC will help to further discriminate mechanistic differences that contribute to the extended control and polymerization of human ACC. DISCUSS | |
| 32 37 human species A comparison between fungal and human ACC will help to further discriminate mechanistic differences that contribute to the extended control and polymerization of human ACC. DISCUSS | |
| 38 41 ACC protein_type A comparison between fungal and human ACC will help to further discriminate mechanistic differences that contribute to the extended control and polymerization of human ACC. DISCUSS | |
| 162 167 human species A comparison between fungal and human ACC will help to further discriminate mechanistic differences that contribute to the extended control and polymerization of human ACC. DISCUSS | |
| 168 171 ACC protein_type A comparison between fungal and human ACC will help to further discriminate mechanistic differences that contribute to the extended control and polymerization of human ACC. DISCUSS | |
| 17 34 crystal structure evidence Most recently, a crystal structure of near full-length non-phosphorylated ACC from S. cerevisae (lacking only 21 N-terminal amino acids, here denoted as flACC) was published by Wei and Tong. DISCUSS | |
| 38 54 near full-length protein_state Most recently, a crystal structure of near full-length non-phosphorylated ACC from S. cerevisae (lacking only 21 N-terminal amino acids, here denoted as flACC) was published by Wei and Tong. DISCUSS | |
| 55 73 non-phosphorylated protein_state Most recently, a crystal structure of near full-length non-phosphorylated ACC from S. cerevisae (lacking only 21 N-terminal amino acids, here denoted as flACC) was published by Wei and Tong. DISCUSS | |
| 74 77 ACC protein_type Most recently, a crystal structure of near full-length non-phosphorylated ACC from S. cerevisae (lacking only 21 N-terminal amino acids, here denoted as flACC) was published by Wei and Tong. DISCUSS | |
| 83 95 S. cerevisae species Most recently, a crystal structure of near full-length non-phosphorylated ACC from S. cerevisae (lacking only 21 N-terminal amino acids, here denoted as flACC) was published by Wei and Tong. DISCUSS | |
| 97 109 lacking only protein_state Most recently, a crystal structure of near full-length non-phosphorylated ACC from S. cerevisae (lacking only 21 N-terminal amino acids, here denoted as flACC) was published by Wei and Tong. DISCUSS | |
| 110 112 21 residue_range Most recently, a crystal structure of near full-length non-phosphorylated ACC from S. cerevisae (lacking only 21 N-terminal amino acids, here denoted as flACC) was published by Wei and Tong. DISCUSS | |
| 153 158 flACC mutant Most recently, a crystal structure of near full-length non-phosphorylated ACC from S. cerevisae (lacking only 21 N-terminal amino acids, here denoted as flACC) was published by Wei and Tong. DISCUSS | |
| 3 8 flACC mutant In flACC, the ACC dimer obeys twofold symmetry and assembles in a triangular architecture with dimeric BC domains (Supplementary Fig. 5a). DISCUSS | |
| 14 17 ACC protein_type In flACC, the ACC dimer obeys twofold symmetry and assembles in a triangular architecture with dimeric BC domains (Supplementary Fig. 5a). DISCUSS | |
| 18 23 dimer oligomeric_state In flACC, the ACC dimer obeys twofold symmetry and assembles in a triangular architecture with dimeric BC domains (Supplementary Fig. 5a). DISCUSS | |
| 66 89 triangular architecture protein_state In flACC, the ACC dimer obeys twofold symmetry and assembles in a triangular architecture with dimeric BC domains (Supplementary Fig. 5a). DISCUSS | |
| 95 102 dimeric oligomeric_state In flACC, the ACC dimer obeys twofold symmetry and assembles in a triangular architecture with dimeric BC domains (Supplementary Fig. 5a). DISCUSS | |
| 103 105 BC structure_element In flACC, the ACC dimer obeys twofold symmetry and assembles in a triangular architecture with dimeric BC domains (Supplementary Fig. 5a). DISCUSS | |
| 16 31 mutational data experimental_method In their study, mutational data indicate a requirement for BC dimerization for catalytic activity. DISCUSS | |
| 24 44 elongated open shape protein_state The transition from the elongated open shape, observed in our experiments, towards a compact triangular shape is based on an intricate interplay of several hinge-bending motions in the CD (Fig. 4d). DISCUSS | |
| 85 109 compact triangular shape protein_state The transition from the elongated open shape, observed in our experiments, towards a compact triangular shape is based on an intricate interplay of several hinge-bending motions in the CD (Fig. 4d). DISCUSS | |
| 185 187 CD structure_element The transition from the elongated open shape, observed in our experiments, towards a compact triangular shape is based on an intricate interplay of several hinge-bending motions in the CD (Fig. 4d). DISCUSS | |
| 0 10 Comparison experimental_method Comparison of flACC with our CthΔBCCP structure reveals the CDC2/CT hinge as a major contributor to conformational flexibility (Supplementary Fig. 5b,c). DISCUSS | |
| 14 19 flACC mutant Comparison of flACC with our CthΔBCCP structure reveals the CDC2/CT hinge as a major contributor to conformational flexibility (Supplementary Fig. 5b,c). DISCUSS | |
| 29 37 CthΔBCCP mutant Comparison of flACC with our CthΔBCCP structure reveals the CDC2/CT hinge as a major contributor to conformational flexibility (Supplementary Fig. 5b,c). DISCUSS | |
| 38 47 structure evidence Comparison of flACC with our CthΔBCCP structure reveals the CDC2/CT hinge as a major contributor to conformational flexibility (Supplementary Fig. 5b,c). DISCUSS | |
| 60 73 CDC2/CT hinge structure_element Comparison of flACC with our CthΔBCCP structure reveals the CDC2/CT hinge as a major contributor to conformational flexibility (Supplementary Fig. 5b,c). DISCUSS | |
| 3 8 flACC mutant In flACC, CDC2 rotates ∼120° with respect to the CT domain. DISCUSS | |
| 10 14 CDC2 structure_element In flACC, CDC2 rotates ∼120° with respect to the CT domain. DISCUSS | |
| 49 51 CT structure_element In flACC, CDC2 rotates ∼120° with respect to the CT domain. DISCUSS | |
| 2 14 second hinge structure_element A second hinge can be identified between CDC1/CDC2. DISCUSS | |
| 41 45 CDC1 structure_element A second hinge can be identified between CDC1/CDC2. DISCUSS | |
| 46 50 CDC2 structure_element A second hinge can be identified between CDC1/CDC2. DISCUSS | |
| 18 31 superposition experimental_method On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 35 39 CDC2 structure_element On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 41 45 CDC1 structure_element On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 53 67 phosphorylated protein_state On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 68 71 Sce species On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 71 73 CD structure_element On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 104 108 CDC1 structure_element On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 116 134 non-phosphorylated protein_state On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 135 140 flACC mutant On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 207 225 non-phosphorylated protein_state On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 226 234 HsaBT-CD mutant On the basis of a superposition of CDC2, CDC1 of the phosphorylated SceCD is rotated by 30° relative to CDC1 of the non-phosphorylated flACC (Supplementary Fig. 5d), similar to what we have observed for the non-phosphorylated HsaBT-CD (Supplementary Fig. 1d). DISCUSS | |
| 5 15 inspecting experimental_method When inspecting all individual protomer and fragment structures in their study, Wei and Tong also identify the CDN/CDC1 connection as a highly flexible hinge, in agreement with our observations. DISCUSS | |
| 31 39 protomer oligomeric_state When inspecting all individual protomer and fragment structures in their study, Wei and Tong also identify the CDN/CDC1 connection as a highly flexible hinge, in agreement with our observations. DISCUSS | |
| 44 52 fragment mutant When inspecting all individual protomer and fragment structures in their study, Wei and Tong also identify the CDN/CDC1 connection as a highly flexible hinge, in agreement with our observations. DISCUSS | |
| 53 63 structures evidence When inspecting all individual protomer and fragment structures in their study, Wei and Tong also identify the CDN/CDC1 connection as a highly flexible hinge, in agreement with our observations. DISCUSS | |
| 111 130 CDN/CDC1 connection structure_element When inspecting all individual protomer and fragment structures in their study, Wei and Tong also identify the CDN/CDC1 connection as a highly flexible hinge, in agreement with our observations. DISCUSS | |
| 136 151 highly flexible protein_state When inspecting all individual protomer and fragment structures in their study, Wei and Tong also identify the CDN/CDC1 connection as a highly flexible hinge, in agreement with our observations. DISCUSS | |
| 152 157 hinge structure_element When inspecting all individual protomer and fragment structures in their study, Wei and Tong also identify the CDN/CDC1 connection as a highly flexible hinge, in agreement with our observations. DISCUSS | |
| 19 29 regulatory protein_state The only bona fide regulatory phophorylation site of fungal ACC in the regulatory loop is directly participating in CDC1/CDC2 domain interactions and thus stabilizes the hinge conformation. DISCUSS | |
| 30 49 phophorylation site site The only bona fide regulatory phophorylation site of fungal ACC in the regulatory loop is directly participating in CDC1/CDC2 domain interactions and thus stabilizes the hinge conformation. DISCUSS | |
| 53 59 fungal taxonomy_domain The only bona fide regulatory phophorylation site of fungal ACC in the regulatory loop is directly participating in CDC1/CDC2 domain interactions and thus stabilizes the hinge conformation. DISCUSS | |
| 60 63 ACC protein_type The only bona fide regulatory phophorylation site of fungal ACC in the regulatory loop is directly participating in CDC1/CDC2 domain interactions and thus stabilizes the hinge conformation. DISCUSS | |
| 71 86 regulatory loop structure_element The only bona fide regulatory phophorylation site of fungal ACC in the regulatory loop is directly participating in CDC1/CDC2 domain interactions and thus stabilizes the hinge conformation. DISCUSS | |
| 116 120 CDC1 structure_element The only bona fide regulatory phophorylation site of fungal ACC in the regulatory loop is directly participating in CDC1/CDC2 domain interactions and thus stabilizes the hinge conformation. DISCUSS | |
| 121 125 CDC2 structure_element The only bona fide regulatory phophorylation site of fungal ACC in the regulatory loop is directly participating in CDC1/CDC2 domain interactions and thus stabilizes the hinge conformation. DISCUSS | |
| 170 188 hinge conformation structure_element The only bona fide regulatory phophorylation site of fungal ACC in the regulatory loop is directly participating in CDC1/CDC2 domain interactions and thus stabilizes the hinge conformation. DISCUSS | |
| 3 8 flACC mutant In flACC, the regulatory loop is mostly disordered, illustrating the increased flexibility due to the absence of the phosphoryl group. DISCUSS | |
| 14 29 regulatory loop structure_element In flACC, the regulatory loop is mostly disordered, illustrating the increased flexibility due to the absence of the phosphoryl group. DISCUSS | |
| 33 50 mostly disordered protein_state In flACC, the regulatory loop is mostly disordered, illustrating the increased flexibility due to the absence of the phosphoryl group. DISCUSS | |
| 117 127 phosphoryl chemical In flACC, the regulatory loop is mostly disordered, illustrating the increased flexibility due to the absence of the phosphoryl group. DISCUSS | |
| 36 45 protomers oligomeric_state Only in three out of eight observed protomers a short peptide stretch (including Ser1157) was modelled. DISCUSS | |
| 48 61 short peptide structure_element Only in three out of eight observed protomers a short peptide stretch (including Ser1157) was modelled. DISCUSS | |
| 81 88 Ser1157 residue_name_number Only in three out of eight observed protomers a short peptide stretch (including Ser1157) was modelled. DISCUSS | |
| 94 102 modelled evidence Only in three out of eight observed protomers a short peptide stretch (including Ser1157) was modelled. DISCUSS | |
| 23 30 Ser1157 residue_name_number In those instances the Ser1157 residue is located at a distance of 14–20 Å away from the location of the phosphorylated serine observed here, based on superposition of either CDC1 or CDC2. DISCUSS | |
| 105 119 phosphorylated protein_state In those instances the Ser1157 residue is located at a distance of 14–20 Å away from the location of the phosphorylated serine observed here, based on superposition of either CDC1 or CDC2. DISCUSS | |
| 120 126 serine residue_name In those instances the Ser1157 residue is located at a distance of 14–20 Å away from the location of the phosphorylated serine observed here, based on superposition of either CDC1 or CDC2. DISCUSS | |
| 151 164 superposition experimental_method In those instances the Ser1157 residue is located at a distance of 14–20 Å away from the location of the phosphorylated serine observed here, based on superposition of either CDC1 or CDC2. DISCUSS | |
| 175 179 CDC1 structure_element In those instances the Ser1157 residue is located at a distance of 14–20 Å away from the location of the phosphorylated serine observed here, based on superposition of either CDC1 or CDC2. DISCUSS | |
| 183 187 CDC2 structure_element In those instances the Ser1157 residue is located at a distance of 14–20 Å away from the location of the phosphorylated serine observed here, based on superposition of either CDC1 or CDC2. DISCUSS | |
| 0 8 Applying experimental_method Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 33 48 CDC1/CDC2 hinge structure_element Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 61 64 Sce species Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 64 66 CD structure_element Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 70 75 flACC mutant Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 85 88 CDN structure_element Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 114 118 CDC2 structure_element Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 123 125 BT structure_element Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 126 129 CDN structure_element Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 144 146 CT structure_element Applying the conformation of the CDC1/CDC2 hinge observed in SceCD on flACC leads to CDN sterically clashing with CDC2 and BT/CDN clashing with CT (Supplementary Fig. 6a,b). DISCUSS | |
| 53 68 phosphorylation ptm Thus, in accordance with the results presented here, phosphorylation of Ser1157 in SceACC most likely limits flexibility in the CDC1/CDC2 hinge such that activation through BC dimerization is not possible (Fig. 4d), which however does not exclude intermolecular dimerization. DISCUSS | |
| 72 79 Ser1157 residue_name_number Thus, in accordance with the results presented here, phosphorylation of Ser1157 in SceACC most likely limits flexibility in the CDC1/CDC2 hinge such that activation through BC dimerization is not possible (Fig. 4d), which however does not exclude intermolecular dimerization. DISCUSS | |
| 83 89 SceACC protein Thus, in accordance with the results presented here, phosphorylation of Ser1157 in SceACC most likely limits flexibility in the CDC1/CDC2 hinge such that activation through BC dimerization is not possible (Fig. 4d), which however does not exclude intermolecular dimerization. DISCUSS | |
| 128 143 CDC1/CDC2 hinge structure_element Thus, in accordance with the results presented here, phosphorylation of Ser1157 in SceACC most likely limits flexibility in the CDC1/CDC2 hinge such that activation through BC dimerization is not possible (Fig. 4d), which however does not exclude intermolecular dimerization. DISCUSS | |
| 173 175 BC structure_element Thus, in accordance with the results presented here, phosphorylation of Ser1157 in SceACC most likely limits flexibility in the CDC1/CDC2 hinge such that activation through BC dimerization is not possible (Fig. 4d), which however does not exclude intermolecular dimerization. DISCUSS | |
| 13 15 EM experimental_method In addition, EM micrographs of phosphorylated and dephosphorylated SceACC display for both samples mainly elongated and U-shaped conformations and reveal no apparent differences in particle shape distributions (Supplementary Fig. 7). DISCUSS | |
| 16 27 micrographs evidence In addition, EM micrographs of phosphorylated and dephosphorylated SceACC display for both samples mainly elongated and U-shaped conformations and reveal no apparent differences in particle shape distributions (Supplementary Fig. 7). DISCUSS | |
| 31 45 phosphorylated protein_state In addition, EM micrographs of phosphorylated and dephosphorylated SceACC display for both samples mainly elongated and U-shaped conformations and reveal no apparent differences in particle shape distributions (Supplementary Fig. 7). DISCUSS | |
| 50 66 dephosphorylated protein_state In addition, EM micrographs of phosphorylated and dephosphorylated SceACC display for both samples mainly elongated and U-shaped conformations and reveal no apparent differences in particle shape distributions (Supplementary Fig. 7). DISCUSS | |
| 67 73 SceACC protein In addition, EM micrographs of phosphorylated and dephosphorylated SceACC display for both samples mainly elongated and U-shaped conformations and reveal no apparent differences in particle shape distributions (Supplementary Fig. 7). DISCUSS | |
| 106 142 elongated and U-shaped conformations protein_state In addition, EM micrographs of phosphorylated and dephosphorylated SceACC display for both samples mainly elongated and U-shaped conformations and reveal no apparent differences in particle shape distributions (Supplementary Fig. 7). DISCUSS | |
| 181 209 particle shape distributions evidence In addition, EM micrographs of phosphorylated and dephosphorylated SceACC display for both samples mainly elongated and U-shaped conformations and reveal no apparent differences in particle shape distributions (Supplementary Fig. 7). DISCUSS | |
| 25 41 triangular shape protein_state This implicates that the triangular shape with dimeric BC domains has a low population also in the active form, even though a biasing influence of grid preparation cannot be excluded completely. DISCUSS | |
| 47 54 dimeric oligomeric_state This implicates that the triangular shape with dimeric BC domains has a low population also in the active form, even though a biasing influence of grid preparation cannot be excluded completely. DISCUSS | |
| 55 57 BC structure_element This implicates that the triangular shape with dimeric BC domains has a low population also in the active form, even though a biasing influence of grid preparation cannot be excluded completely. DISCUSS | |
| 99 110 active form protein_state This implicates that the triangular shape with dimeric BC domains has a low population also in the active form, even though a biasing influence of grid preparation cannot be excluded completely. DISCUSS | |
| 76 110 carrier protein-based multienzymes protein_type Large-scale conformational variability has also been observed in most other carrier protein-based multienzymes, including polyketide and fatty-acid synthases (with the exception of fungal-type fatty-acid synthases), non-ribosomal peptide synthetases and the pyruvate dehydrogenase complexes, although based on completely different architectures. DISCUSS | |
| 122 157 polyketide and fatty-acid synthases protein_type Large-scale conformational variability has also been observed in most other carrier protein-based multienzymes, including polyketide and fatty-acid synthases (with the exception of fungal-type fatty-acid synthases), non-ribosomal peptide synthetases and the pyruvate dehydrogenase complexes, although based on completely different architectures. DISCUSS | |
| 181 213 fungal-type fatty-acid synthases protein_type Large-scale conformational variability has also been observed in most other carrier protein-based multienzymes, including polyketide and fatty-acid synthases (with the exception of fungal-type fatty-acid synthases), non-ribosomal peptide synthetases and the pyruvate dehydrogenase complexes, although based on completely different architectures. DISCUSS | |
| 216 249 non-ribosomal peptide synthetases protein_type Large-scale conformational variability has also been observed in most other carrier protein-based multienzymes, including polyketide and fatty-acid synthases (with the exception of fungal-type fatty-acid synthases), non-ribosomal peptide synthetases and the pyruvate dehydrogenase complexes, although based on completely different architectures. DISCUSS | |
| 258 290 pyruvate dehydrogenase complexes protein_type Large-scale conformational variability has also been observed in most other carrier protein-based multienzymes, including polyketide and fatty-acid synthases (with the exception of fungal-type fatty-acid synthases), non-ribosomal peptide synthetases and the pyruvate dehydrogenase complexes, although based on completely different architectures. DISCUSS | |
| 15 37 structural information evidence Together, this structural information suggests that variable carrier protein tethering is not sufficient for efficient substrate transfer and catalysis in any of these systems. DISCUSS | |
| 4 29 determination of a set of experimental_method The determination of a set of crystal structures of SceACC in two states, unphosphorylated and phosphorylated at the major regulatory site Ser1157, provides a unique depiction of multienzyme regulation by post-translational modification (Fig. 4d). DISCUSS | |
| 30 48 crystal structures evidence The determination of a set of crystal structures of SceACC in two states, unphosphorylated and phosphorylated at the major regulatory site Ser1157, provides a unique depiction of multienzyme regulation by post-translational modification (Fig. 4d). DISCUSS | |
| 52 58 SceACC protein The determination of a set of crystal structures of SceACC in two states, unphosphorylated and phosphorylated at the major regulatory site Ser1157, provides a unique depiction of multienzyme regulation by post-translational modification (Fig. 4d). DISCUSS | |
| 74 90 unphosphorylated protein_state The determination of a set of crystal structures of SceACC in two states, unphosphorylated and phosphorylated at the major regulatory site Ser1157, provides a unique depiction of multienzyme regulation by post-translational modification (Fig. 4d). DISCUSS | |
| 95 109 phosphorylated protein_state The determination of a set of crystal structures of SceACC in two states, unphosphorylated and phosphorylated at the major regulatory site Ser1157, provides a unique depiction of multienzyme regulation by post-translational modification (Fig. 4d). DISCUSS | |
| 117 138 major regulatory site site The determination of a set of crystal structures of SceACC in two states, unphosphorylated and phosphorylated at the major regulatory site Ser1157, provides a unique depiction of multienzyme regulation by post-translational modification (Fig. 4d). DISCUSS | |
| 139 146 Ser1157 residue_name_number The determination of a set of crystal structures of SceACC in two states, unphosphorylated and phosphorylated at the major regulatory site Ser1157, provides a unique depiction of multienzyme regulation by post-translational modification (Fig. 4d). DISCUSS | |
| 4 18 phosphorylated protein_state The phosphorylated regulatory loop binds to an allosteric site at the interface of two non-catalytic domains and restricts conformational freedom at several hinges in the dynamic ACC. DISCUSS | |
| 19 34 regulatory loop structure_element The phosphorylated regulatory loop binds to an allosteric site at the interface of two non-catalytic domains and restricts conformational freedom at several hinges in the dynamic ACC. DISCUSS | |
| 47 62 allosteric site site The phosphorylated regulatory loop binds to an allosteric site at the interface of two non-catalytic domains and restricts conformational freedom at several hinges in the dynamic ACC. DISCUSS | |
| 70 79 interface site The phosphorylated regulatory loop binds to an allosteric site at the interface of two non-catalytic domains and restricts conformational freedom at several hinges in the dynamic ACC. DISCUSS | |
| 87 100 non-catalytic protein_state The phosphorylated regulatory loop binds to an allosteric site at the interface of two non-catalytic domains and restricts conformational freedom at several hinges in the dynamic ACC. DISCUSS | |
| 157 163 hinges structure_element The phosphorylated regulatory loop binds to an allosteric site at the interface of two non-catalytic domains and restricts conformational freedom at several hinges in the dynamic ACC. DISCUSS | |
| 171 178 dynamic protein_state The phosphorylated regulatory loop binds to an allosteric site at the interface of two non-catalytic domains and restricts conformational freedom at several hinges in the dynamic ACC. DISCUSS | |
| 179 182 ACC protein_type The phosphorylated regulatory loop binds to an allosteric site at the interface of two non-catalytic domains and restricts conformational freedom at several hinges in the dynamic ACC. DISCUSS | |
| 32 58 rare, compact conformation protein_state It disfavours the adoption of a rare, compact conformation, in which intramolecular dimerization of the BC domains results in catalytic turnover. DISCUSS | |
| 104 106 BC structure_element It disfavours the adoption of a rare, compact conformation, in which intramolecular dimerization of the BC domains results in catalytic turnover. DISCUSS | |
| 138 159 active site structure site The regulation of activity thus results from restrained large-scale conformational dynamics rather than a direct or indirect influence on active site structure. DISCUSS | |
| 23 26 ACC protein_type To our best knowledge, ACC is the first multienzyme for which such a phosphorylation-dependent mechanical control mechanism has been visualized. DISCUSS | |
| 40 51 multienzyme protein_type To our best knowledge, ACC is the first multienzyme for which such a phosphorylation-dependent mechanical control mechanism has been visualized. DISCUSS | |
| 69 84 phosphorylation ptm To our best knowledge, ACC is the first multienzyme for which such a phosphorylation-dependent mechanical control mechanism has been visualized. DISCUSS | |
| 24 27 ACC protein_type However, the example of ACC now demonstrates the possibility of regulating activity by controlled dynamics of non-enzymatic linker regions also in other families of carrier-dependent multienzymes. DISCUSS | |
| 110 138 non-enzymatic linker regions structure_element However, the example of ACC now demonstrates the possibility of regulating activity by controlled dynamics of non-enzymatic linker regions also in other families of carrier-dependent multienzymes. DISCUSS | |
| 165 195 carrier-dependent multienzymes protein_type However, the example of ACC now demonstrates the possibility of regulating activity by controlled dynamics of non-enzymatic linker regions also in other families of carrier-dependent multienzymes. DISCUSS | |
| 4 18 phosphorylated protein_state The phosphorylated central domain of yeast ACC. FIG | |
| 19 33 central domain structure_element The phosphorylated central domain of yeast ACC. FIG | |
| 37 42 yeast taxonomy_domain The phosphorylated central domain of yeast ACC. FIG | |
| 43 46 ACC protein_type The phosphorylated central domain of yeast ACC. FIG | |
| 53 63 eukaryotic taxonomy_domain (a) Schematic overview of the domain organization of eukaryotic ACCs. FIG | |
| 64 68 ACCs protein_type (a) Schematic overview of the domain organization of eukaryotic ACCs. FIG | |
| 0 23 Crystallized constructs evidence Crystallized constructs are indicated. FIG | |
| 34 37 Sce species (b) Cartoon representation of the SceCD crystal structure. FIG | |
| 37 39 CD structure_element (b) Cartoon representation of the SceCD crystal structure. FIG | |
| 40 57 crystal structure evidence (b) Cartoon representation of the SceCD crystal structure. FIG | |
| 0 3 CDN structure_element CDN is linked by a four-helix bundle (CDL) to two α–β-fold domains (CDC1 and CDC2). FIG | |
| 19 36 four-helix bundle structure_element CDN is linked by a four-helix bundle (CDL) to two α–β-fold domains (CDC1 and CDC2). FIG | |
| 38 41 CDL structure_element CDN is linked by a four-helix bundle (CDL) to two α–β-fold domains (CDC1 and CDC2). FIG | |
| 46 66 two α–β-fold domains structure_element CDN is linked by a four-helix bundle (CDL) to two α–β-fold domains (CDC1 and CDC2). FIG | |
| 68 72 CDC1 structure_element CDN is linked by a four-helix bundle (CDL) to two α–β-fold domains (CDC1 and CDC2). FIG | |
| 77 81 CDC2 structure_element CDN is linked by a four-helix bundle (CDL) to two α–β-fold domains (CDC1 and CDC2). FIG | |
| 4 19 regulatory loop structure_element The regulatory loop is shown as bold cartoon, and the phosphorylated Ser1157 is marked by a red triangle. FIG | |
| 54 68 phosphorylated protein_state The regulatory loop is shown as bold cartoon, and the phosphorylated Ser1157 is marked by a red triangle. FIG | |
| 69 76 Ser1157 residue_name_number The regulatory loop is shown as bold cartoon, and the phosphorylated Ser1157 is marked by a red triangle. FIG | |
| 4 17 Superposition experimental_method (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 21 25 CDC1 structure_element (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 30 34 CDC2 structure_element (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 43 59 highly conserved protein_state (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 60 65 folds structure_element (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 75 90 regulatory loop structure_element (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 100 114 phosphorylated protein_state (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 115 122 Ser1157 residue_name_number (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 155 159 CDC1 structure_element (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 164 168 CDC2 structure_element (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 174 183 conserved protein_state (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 193 200 Arg1173 residue_name_number (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 205 212 Arg1260 residue_name_number (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 228 238 phosphoryl chemical (c) Superposition of CDC1 and CDC2 reveals highly conserved folds. (d) The regulatory loop with the phosphorylated Ser1157 is bound into a crevice between CDC1 and CDC2, the conserved residues Arg1173 and Arg1260 coordinate the phosphoryl-group. FIG | |
| 27 35 HsaBT-CD mutant (e) Structural overview of HsaBT-CD. FIG | |
| 40 44 BCCP structure_element The attachment points to the N-terminal BCCP domain and the C-terminal CT domain are indicated with spheres. FIG | |
| 71 73 CT structure_element The attachment points to the N-terminal BCCP domain and the C-terminal CT domain are indicated with spheres. FIG | |
| 20 22 CD structure_element Architecture of the CD–CT core of fungal ACC. FIG | |
| 23 25 CT structure_element Architecture of the CD–CT core of fungal ACC. FIG | |
| 34 40 fungal taxonomy_domain Architecture of the CD–CT core of fungal ACC. FIG | |
| 41 44 ACC protein_type Architecture of the CD–CT core of fungal ACC. FIG | |
| 26 44 crystal structures evidence Cartoon representation of crystal structures of multidomain constructs of CthACC. FIG | |
| 48 70 multidomain constructs mutant Cartoon representation of crystal structures of multidomain constructs of CthACC. FIG | |
| 74 80 CthACC protein Cartoon representation of crystal structures of multidomain constructs of CthACC. FIG | |
| 4 12 protomer oligomeric_state One protomer is shown in colour and one in grey. FIG | |
| 37 48 active site site Individual domains are labelled; the active site of CT and the position of the conserved regulatory phosphoserine site based on SceCD are indicated by an asterisk and a triangle, respectively. FIG | |
| 52 54 CT structure_element Individual domains are labelled; the active site of CT and the position of the conserved regulatory phosphoserine site based on SceCD are indicated by an asterisk and a triangle, respectively. FIG | |
| 79 88 conserved protein_state Individual domains are labelled; the active site of CT and the position of the conserved regulatory phosphoserine site based on SceCD are indicated by an asterisk and a triangle, respectively. FIG | |
| 89 99 regulatory protein_state Individual domains are labelled; the active site of CT and the position of the conserved regulatory phosphoserine site based on SceCD are indicated by an asterisk and a triangle, respectively. FIG | |
| 100 118 phosphoserine site site Individual domains are labelled; the active site of CT and the position of the conserved regulatory phosphoserine site based on SceCD are indicated by an asterisk and a triangle, respectively. FIG | |
| 128 131 Sce species Individual domains are labelled; the active site of CT and the position of the conserved regulatory phosphoserine site based on SceCD are indicated by an asterisk and a triangle, respectively. FIG | |
| 131 133 CD structure_element Individual domains are labelled; the active site of CT and the position of the conserved regulatory phosphoserine site based on SceCD are indicated by an asterisk and a triangle, respectively. FIG | |
| 34 38 CDC2 structure_element Variability of the connections of CDC2 to CT and CDC1 in fungal ACC. FIG | |
| 42 44 CT structure_element Variability of the connections of CDC2 to CT and CDC1 in fungal ACC. FIG | |
| 49 53 CDC1 structure_element Variability of the connections of CDC2 to CT and CDC1 in fungal ACC. FIG | |
| 57 63 fungal taxonomy_domain Variability of the connections of CDC2 to CT and CDC1 in fungal ACC. FIG | |
| 64 67 ACC protein_type Variability of the connections of CDC2 to CT and CDC1 in fungal ACC. FIG | |
| 4 9 Hinge structure_element (a) Hinge properties of the CDC2–CT connection analysed by a CT-based superposition of eight instances of the CDC2-CT segment. FIG | |
| 28 46 CDC2–CT connection structure_element (a) Hinge properties of the CDC2–CT connection analysed by a CT-based superposition of eight instances of the CDC2-CT segment. FIG | |
| 61 83 CT-based superposition experimental_method (a) Hinge properties of the CDC2–CT connection analysed by a CT-based superposition of eight instances of the CDC2-CT segment. FIG | |
| 110 125 CDC2-CT segment mutant (a) Hinge properties of the CDC2–CT connection analysed by a CT-based superposition of eight instances of the CDC2-CT segment. FIG | |
| 22 30 protomer oligomeric_state For clarity, only one protomer of CthCD-CTCter1 is shown in full colour as reference. FIG | |
| 34 47 CthCD-CTCter1 mutant For clarity, only one protomer of CthCD-CTCter1 is shown in full colour as reference. FIG | |
| 21 25 CDC2 structure_element For other instances, CDC2 domains are shown in transparent tube representation with only one helix each highlighted. FIG | |
| 74 78 CDC2 structure_element The range of hinge bending is indicated and the connection points between CDC2 and CT (blue) as well as between CDC1 and CDC2 (green and grey) are marked as spheres. FIG | |
| 83 85 CT structure_element The range of hinge bending is indicated and the connection points between CDC2 and CT (blue) as well as between CDC1 and CDC2 (green and grey) are marked as spheres. FIG | |
| 112 116 CDC1 structure_element The range of hinge bending is indicated and the connection points between CDC2 and CT (blue) as well as between CDC1 and CDC2 (green and grey) are marked as spheres. FIG | |
| 121 125 CDC2 structure_element The range of hinge bending is indicated and the connection points between CDC2 and CT (blue) as well as between CDC1 and CDC2 (green and grey) are marked as spheres. FIG | |
| 8 29 interdomain interface site (b) The interdomain interface of CDC1 and CDC2 exhibits only limited plasticity. FIG | |
| 33 37 CDC1 structure_element (b) The interdomain interface of CDC1 and CDC2 exhibits only limited plasticity. FIG | |
| 42 46 CDC2 structure_element (b) The interdomain interface of CDC1 and CDC2 exhibits only limited plasticity. FIG | |
| 32 36 CDC1 structure_element Representation as in a, but the CDC1 and CDC2 are superposed based on CDC2. FIG | |
| 41 45 CDC2 structure_element Representation as in a, but the CDC1 and CDC2 are superposed based on CDC2. FIG | |
| 50 60 superposed experimental_method Representation as in a, but the CDC1 and CDC2 are superposed based on CDC2. FIG | |
| 70 74 CDC2 structure_element Representation as in a, but the CDC1 and CDC2 are superposed based on CDC2. FIG | |
| 4 12 protomer oligomeric_state One protomer of CthΔBCCP is shown in colour, the CDL domains are omitted for clarity and the position of the phosphorylated serine based on SceCD is indicated with a red triangle. FIG | |
| 16 24 CthΔBCCP mutant One protomer of CthΔBCCP is shown in colour, the CDL domains are omitted for clarity and the position of the phosphorylated serine based on SceCD is indicated with a red triangle. FIG | |
| 49 52 CDL structure_element One protomer of CthΔBCCP is shown in colour, the CDL domains are omitted for clarity and the position of the phosphorylated serine based on SceCD is indicated with a red triangle. FIG | |
| 109 123 phosphorylated protein_state One protomer of CthΔBCCP is shown in colour, the CDL domains are omitted for clarity and the position of the phosphorylated serine based on SceCD is indicated with a red triangle. FIG | |
| 124 130 serine residue_name One protomer of CthΔBCCP is shown in colour, the CDL domains are omitted for clarity and the position of the phosphorylated serine based on SceCD is indicated with a red triangle. FIG | |
| 140 143 Sce species One protomer of CthΔBCCP is shown in colour, the CDL domains are omitted for clarity and the position of the phosphorylated serine based on SceCD is indicated with a red triangle. FIG | |
| 143 145 CD structure_element One protomer of CthΔBCCP is shown in colour, the CDL domains are omitted for clarity and the position of the phosphorylated serine based on SceCD is indicated with a red triangle. FIG | |
| 27 31 CDC1 structure_element The connection points from CDC1 to CDC2 and to CDL are represented by green spheres. FIG | |
| 35 39 CDC2 structure_element The connection points from CDC1 to CDC2 and to CDL are represented by green spheres. FIG | |
| 47 50 CDL structure_element The connection points from CDC1 to CDC2 and to CDL are represented by green spheres. FIG | |
| 31 37 fungal taxonomy_domain The conformational dynamics of fungal ACC. FIG | |
| 38 41 ACC protein_type The conformational dynamics of fungal ACC. FIG | |
| 52 55 CDN structure_element (a–c) Large-scale conformational variability of the CDN domain relative to the CDL/CDC1 domain. FIG | |
| 79 82 CDL structure_element (a–c) Large-scale conformational variability of the CDN domain relative to the CDL/CDC1 domain. FIG | |
| 83 87 CDC1 structure_element (a–c) Large-scale conformational variability of the CDN domain relative to the CDL/CDC1 domain. FIG | |
| 0 9 CthCD-CT1 mutant CthCD-CT1 (in colour) serves as reference, the compared structures (as indicated, numbers after construct name differentiate between individual protomers) are shown in grey. FIG | |
| 47 66 compared structures experimental_method CthCD-CT1 (in colour) serves as reference, the compared structures (as indicated, numbers after construct name differentiate between individual protomers) are shown in grey. FIG | |
| 144 153 protomers oligomeric_state CthCD-CT1 (in colour) serves as reference, the compared structures (as indicated, numbers after construct name differentiate between individual protomers) are shown in grey. FIG | |
| 19 22 CDN structure_element Domains other than CDN and CDL/CDC1 are omitted for clarity. FIG | |
| 27 30 CDL structure_element Domains other than CDN and CDL/CDC1 are omitted for clarity. FIG | |
| 31 35 CDC1 structure_element Domains other than CDN and CDL/CDC1 are omitted for clarity. FIG | |
| 68 71 CDN structure_element The domains are labelled and the distances between the N termini of CDN (spheres) in the compared structures are indicated. FIG | |
| 23 29 fungal taxonomy_domain (d) Schematic model of fungal ACC showing the intrinsic, regulated flexibility of CD in the phosphorylated inhibited or the non-phosphorylated activated state. FIG | |
| 30 33 ACC protein_type (d) Schematic model of fungal ACC showing the intrinsic, regulated flexibility of CD in the phosphorylated inhibited or the non-phosphorylated activated state. FIG | |
| 82 84 CD structure_element (d) Schematic model of fungal ACC showing the intrinsic, regulated flexibility of CD in the phosphorylated inhibited or the non-phosphorylated activated state. FIG | |
| 92 106 phosphorylated protein_state (d) Schematic model of fungal ACC showing the intrinsic, regulated flexibility of CD in the phosphorylated inhibited or the non-phosphorylated activated state. FIG | |
| 107 116 inhibited protein_state (d) Schematic model of fungal ACC showing the intrinsic, regulated flexibility of CD in the phosphorylated inhibited or the non-phosphorylated activated state. FIG | |
| 124 142 non-phosphorylated protein_state (d) Schematic model of fungal ACC showing the intrinsic, regulated flexibility of CD in the phosphorylated inhibited or the non-phosphorylated activated state. FIG | |
| 143 152 activated protein_state (d) Schematic model of fungal ACC showing the intrinsic, regulated flexibility of CD in the phosphorylated inhibited or the non-phosphorylated activated state. FIG | |
| 19 23 CDC2 structure_element Flexibility of the CDC2/CT and CDN/CDL hinges is illustrated by arrows. FIG | |
| 24 26 CT structure_element Flexibility of the CDC2/CT and CDN/CDL hinges is illustrated by arrows. FIG | |
| 31 34 CDN structure_element Flexibility of the CDC2/CT and CDN/CDL hinges is illustrated by arrows. FIG | |
| 35 38 CDL structure_element Flexibility of the CDC2/CT and CDN/CDL hinges is illustrated by arrows. FIG | |
| 39 45 hinges structure_element Flexibility of the CDC2/CT and CDN/CDL hinges is illustrated by arrows. FIG | |
| 4 11 Ser1157 residue_name_number The Ser1157 phosphorylation site and the regulatory loop are schematically indicated in magenta. FIG | |
| 12 27 phosphorylation ptm The Ser1157 phosphorylation site and the regulatory loop are schematically indicated in magenta. FIG | |
| 41 56 regulatory loop structure_element The Ser1157 phosphorylation site and the regulatory loop are schematically indicated in magenta. FIG | |