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