diff --git "a/annotation_CSV/PMC4833862.csv" "b/annotation_CSV/PMC4833862.csv"
new file mode 100644--- /dev/null
+++ "b/annotation_CSV/PMC4833862.csv"
@@ -0,0 +1,1045 @@
+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