anno_start	anno_end	anno_text	entity_type	sentence	section
4	27	immunity-related GTPase	protein_type	The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion	TITLE
28	33	Irga6	protein	The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion	TITLE
34	43	dimerizes	oligomeric_state	The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion	TITLE
49	70	parallel head-to-head	protein_state	The immunity-related GTPase Irga6 dimerizes in a parallel head-to-head fashion	TITLE
4	28	immunity-related GTPases	protein_type	The immunity-related GTPases (IRGs) constitute a powerful cell-autonomous resistance system against several intracellular pathogens.	ABSTRACT
30	34	IRGs	protein_type	The immunity-related GTPases (IRGs) constitute a powerful cell-autonomous resistance system against several intracellular pathogens.	ABSTRACT
0	5	Irga6	protein	Irga6 is a dynamin-like protein that oligomerizes at the parasitophorous vacuolar membrane (PVM) of Toxoplasma gondii leading to its vesiculation.	ABSTRACT
11	31	dynamin-like protein	protein_type	Irga6 is a dynamin-like protein that oligomerizes at the parasitophorous vacuolar membrane (PVM) of Toxoplasma gondii leading to its vesiculation.	ABSTRACT
100	117	Toxoplasma gondii	species	Irga6 is a dynamin-like protein that oligomerizes at the parasitophorous vacuolar membrane (PVM) of Toxoplasma gondii leading to its vesiculation.	ABSTRACT
20	40	biochemical analysis	experimental_method	Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization.	ABSTRACT
72	86	GTPase domains	structure_element	Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization.	ABSTRACT
90	95	Irga6	protein	Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization.	ABSTRACT
96	104	dimerize	oligomeric_state	Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization.	ABSTRACT
111	123	antiparallel	protein_state	Based on a previous biochemical analysis, it has been proposed that the GTPase domains of Irga6 dimerize in an antiparallel fashion during oligomerization.	ABSTRACT
3	13	determined	experimental_method	We determined the crystal structure of an oligomerization-impaired Irga6 mutant bound to a non-hydrolyzable GTP analog.	ABSTRACT
18	35	crystal structure	evidence	We determined the crystal structure of an oligomerization-impaired Irga6 mutant bound to a non-hydrolyzable GTP analog.	ABSTRACT
42	66	oligomerization-impaired	protein_state	We determined the crystal structure of an oligomerization-impaired Irga6 mutant bound to a non-hydrolyzable GTP analog.	ABSTRACT
67	72	Irga6	protein	We determined the crystal structure of an oligomerization-impaired Irga6 mutant bound to a non-hydrolyzable GTP analog.	ABSTRACT
73	79	mutant	protein_state	We determined the crystal structure of an oligomerization-impaired Irga6 mutant bound to a non-hydrolyzable GTP analog.	ABSTRACT
80	88	bound to	protein_state	We determined the crystal structure of an oligomerization-impaired Irga6 mutant bound to a non-hydrolyzable GTP analog.	ABSTRACT
108	111	GTP	chemical	We determined the crystal structure of an oligomerization-impaired Irga6 mutant bound to a non-hydrolyzable GTP analog.	ABSTRACT
36	45	structure	evidence	Contrary to the previous model, the structure shows that the GTPase domains dimerize in a parallel fashion.	ABSTRACT
61	75	GTPase domains	structure_element	Contrary to the previous model, the structure shows that the GTPase domains dimerize in a parallel fashion.	ABSTRACT
76	84	dimerize	oligomeric_state	Contrary to the previous model, the structure shows that the GTPase domains dimerize in a parallel fashion.	ABSTRACT
90	98	parallel	protein_state	Contrary to the previous model, the structure shows that the GTPase domains dimerize in a parallel fashion.	ABSTRACT
4	15	nucleotides	chemical	The nucleotides in the center of the interface participate in dimerization by forming symmetric contacts with each other and with the switch I region of the opposing Irga6 molecule.	ABSTRACT
37	46	interface	site	The nucleotides in the center of the interface participate in dimerization by forming symmetric contacts with each other and with the switch I region of the opposing Irga6 molecule.	ABSTRACT
134	142	switch I	site	The nucleotides in the center of the interface participate in dimerization by forming symmetric contacts with each other and with the switch I region of the opposing Irga6 molecule.	ABSTRACT
166	171	Irga6	protein	The nucleotides in the center of the interface participate in dimerization by forming symmetric contacts with each other and with the switch I region of the opposing Irga6 molecule.	ABSTRACT
39	42	GTP	chemical	The latter contact appears to activate GTP hydrolysis by stabilizing the position of the catalytic glutamate 106 in switch I close to the active site.	ABSTRACT
89	98	catalytic	protein_state	The latter contact appears to activate GTP hydrolysis by stabilizing the position of the catalytic glutamate 106 in switch I close to the active site.	ABSTRACT
99	112	glutamate 106	residue_name_number	The latter contact appears to activate GTP hydrolysis by stabilizing the position of the catalytic glutamate 106 in switch I close to the active site.	ABSTRACT
116	124	switch I	site	The latter contact appears to activate GTP hydrolysis by stabilizing the position of the catalytic glutamate 106 in switch I close to the active site.	ABSTRACT
138	149	active site	site	The latter contact appears to activate GTP hydrolysis by stabilizing the position of the catalytic glutamate 106 in switch I close to the active site.	ABSTRACT
38	47	switch II	site	Further dimerization contacts involve switch II, the G4 helix and the trans stabilizing loop.	ABSTRACT
53	61	G4 helix	structure_element	Further dimerization contacts involve switch II, the G4 helix and the trans stabilizing loop.	ABSTRACT
70	92	trans stabilizing loop	structure_element	Further dimerization contacts involve switch II, the G4 helix and the trans stabilizing loop.	ABSTRACT
4	9	Irga6	protein	The Irga6 structure features a parallel GTPase domain dimer, which appears to be a unifying feature of all dynamin and septin superfamily members.	ABSTRACT
10	19	structure	evidence	The Irga6 structure features a parallel GTPase domain dimer, which appears to be a unifying feature of all dynamin and septin superfamily members.	ABSTRACT
31	39	parallel	protein_state	The Irga6 structure features a parallel GTPase domain dimer, which appears to be a unifying feature of all dynamin and septin superfamily members.	ABSTRACT
40	53	GTPase domain	structure_element	The Irga6 structure features a parallel GTPase domain dimer, which appears to be a unifying feature of all dynamin and septin superfamily members.	ABSTRACT
54	59	dimer	oligomeric_state	The Irga6 structure features a parallel GTPase domain dimer, which appears to be a unifying feature of all dynamin and septin superfamily members.	ABSTRACT
107	114	dynamin	protein_type	The Irga6 structure features a parallel GTPase domain dimer, which appears to be a unifying feature of all dynamin and septin superfamily members.	ABSTRACT
119	125	septin	protein_type	The Irga6 structure features a parallel GTPase domain dimer, which appears to be a unifying feature of all dynamin and septin superfamily members.	ABSTRACT
88	91	IRG	protein_type	This study contributes important insights into the assembly and catalytic mechanisms of IRG proteins as prerequisite to understand their anti-microbial action.	ABSTRACT
0	24	Immunity-related GTPases	protein_type	Immunity-related GTPases (IRGs) comprise a family of dynamin-related cell-autonomous resistance proteins targeting intracellular pathogens, such as Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Trypanosoma cruzi, and Toxoplasma gondii.	INTRO
26	30	IRGs	protein_type	Immunity-related GTPases (IRGs) comprise a family of dynamin-related cell-autonomous resistance proteins targeting intracellular pathogens, such as Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Trypanosoma cruzi, and Toxoplasma gondii.	INTRO
53	104	dynamin-related cell-autonomous resistance proteins	protein_type	Immunity-related GTPases (IRGs) comprise a family of dynamin-related cell-autonomous resistance proteins targeting intracellular pathogens, such as Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Trypanosoma cruzi, and Toxoplasma gondii.	INTRO
148	174	Mycobacterium tuberculosis	species	Immunity-related GTPases (IRGs) comprise a family of dynamin-related cell-autonomous resistance proteins targeting intracellular pathogens, such as Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Trypanosoma cruzi, and Toxoplasma gondii.	INTRO
176	195	Mycobacterium avium	species	Immunity-related GTPases (IRGs) comprise a family of dynamin-related cell-autonomous resistance proteins targeting intracellular pathogens, such as Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Trypanosoma cruzi, and Toxoplasma gondii.	INTRO
197	219	Listeria monocytogenes	species	Immunity-related GTPases (IRGs) comprise a family of dynamin-related cell-autonomous resistance proteins targeting intracellular pathogens, such as Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Trypanosoma cruzi, and Toxoplasma gondii.	INTRO
221	238	Trypanosoma cruzi	species	Immunity-related GTPases (IRGs) comprise a family of dynamin-related cell-autonomous resistance proteins targeting intracellular pathogens, such as Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Trypanosoma cruzi, and Toxoplasma gondii.	INTRO
244	261	Toxoplasma gondii	species	Immunity-related GTPases (IRGs) comprise a family of dynamin-related cell-autonomous resistance proteins targeting intracellular pathogens, such as Mycobacterium tuberculosis, Mycobacterium avium, Listeria monocytogenes, Trypanosoma cruzi, and Toxoplasma gondii.	INTRO
3	7	mice	taxonomy_domain	In mice, the 23 IRG members are induced by interferons, whereas the single human homologue is constitutively expressed in some tissues, especially in testis.	INTRO
16	19	IRG	protein_type	In mice, the 23 IRG members are induced by interferons, whereas the single human homologue is constitutively expressed in some tissues, especially in testis.	INTRO
43	54	interferons	protein_type	In mice, the 23 IRG members are induced by interferons, whereas the single human homologue is constitutively expressed in some tissues, especially in testis.	INTRO
75	80	human	species	In mice, the 23 IRG members are induced by interferons, whereas the single human homologue is constitutively expressed in some tissues, especially in testis.	INTRO
28	32	IRGs	protein_type	In non-infected cells, most IRGs are largely cytosolic.	INTRO
13	17	IRGs	protein_type	In this way, IRGs contribute to the release of the pathogen into the cytoplasm and its subsequent destruction.	INTRO
0	5	Irga6	protein	Irga6, one of the effector IRG proteins, localizes to the intact parasitophorous vacuole membrane (PVM) and, after disruption of the PVM, is found associated with vesicular accumulations, presumably derived from the PVM.	INTRO
27	30	IRG	protein_type	Irga6, one of the effector IRG proteins, localizes to the intact parasitophorous vacuole membrane (PVM) and, after disruption of the PVM, is found associated with vesicular accumulations, presumably derived from the PVM.	INTRO
2	21	myristoylation site	site	A myristoylation site at Gly2 is necessary for the recruitment to the PVM but not for the weak constitutive binding to the ER membrane.	INTRO
25	29	Gly2	residue_name_number	A myristoylation site at Gly2 is necessary for the recruitment to the PVM but not for the weak constitutive binding to the ER membrane.	INTRO
43	50	helix A	structure_element	An internally oriented antibody epitope on helix A between positions 20 and 24 was demonstrated to be accessible in the GTP-, but not in the GDP-bound state.	INTRO
69	78	20 and 24	residue_range	An internally oriented antibody epitope on helix A between positions 20 and 24 was demonstrated to be accessible in the GTP-, but not in the GDP-bound state.	INTRO
120	125	GTP-,	protein_state	An internally oriented antibody epitope on helix A between positions 20 and 24 was demonstrated to be accessible in the GTP-, but not in the GDP-bound state.	INTRO
141	150	GDP-bound	protein_state	An internally oriented antibody epitope on helix A between positions 20 and 24 was demonstrated to be accessible in the GTP-, but not in the GDP-bound state.	INTRO
51	54	GTP	chemical	This indicates large-scale structural changes upon GTP binding that probably include exposure of the myristoyl group, enhancing binding to the PVM.	INTRO
0	19	Biochemical studies	experimental_method	Biochemical studies indicated that Irga6 hydrolyses GTP in a cooperative manner and forms GTP-dependent oligomers in vitro and in vivo.	INTRO
35	40	Irga6	protein	Biochemical studies indicated that Irga6 hydrolyses GTP in a cooperative manner and forms GTP-dependent oligomers in vitro and in vivo.	INTRO
52	55	GTP	chemical	Biochemical studies indicated that Irga6 hydrolyses GTP in a cooperative manner and forms GTP-dependent oligomers in vitro and in vivo.	INTRO
90	103	GTP-dependent	protein_state	Biochemical studies indicated that Irga6 hydrolyses GTP in a cooperative manner and forms GTP-dependent oligomers in vitro and in vivo.	INTRO
104	113	oligomers	oligomeric_state	Biochemical studies indicated that Irga6 hydrolyses GTP in a cooperative manner and forms GTP-dependent oligomers in vitro and in vivo.	INTRO
0	18	Crystal structures	evidence	Crystal structures of Irga6 in various nucleotide-loaded states revealed the basic architecture of IRG proteins, including a GTPase domain and a composite helical domain.	INTRO
22	27	Irga6	protein	Crystal structures of Irga6 in various nucleotide-loaded states revealed the basic architecture of IRG proteins, including a GTPase domain and a composite helical domain.	INTRO
39	56	nucleotide-loaded	protein_state	Crystal structures of Irga6 in various nucleotide-loaded states revealed the basic architecture of IRG proteins, including a GTPase domain and a composite helical domain.	INTRO
99	102	IRG	protein_type	Crystal structures of Irga6 in various nucleotide-loaded states revealed the basic architecture of IRG proteins, including a GTPase domain and a composite helical domain.	INTRO
125	138	GTPase domain	structure_element	Crystal structures of Irga6 in various nucleotide-loaded states revealed the basic architecture of IRG proteins, including a GTPase domain and a composite helical domain.	INTRO
145	169	composite helical domain	structure_element	Crystal structures of Irga6 in various nucleotide-loaded states revealed the basic architecture of IRG proteins, including a GTPase domain and a composite helical domain.	INTRO
36	58	dimerization interface	site	These studies additionally showed a dimerization interface in the nucleotide-free protein as well as in all nucleotide-bound states.	INTRO
66	81	nucleotide-free	protein_state	These studies additionally showed a dimerization interface in the nucleotide-free protein as well as in all nucleotide-bound states.	INTRO
108	124	nucleotide-bound	protein_state	These studies additionally showed a dimerization interface in the nucleotide-free protein as well as in all nucleotide-bound states.	INTRO
14	35	GTPase domain surface	site	It involves a GTPase domain surface, which is located at the opposite side of the nucleotide, and an interface in the helical domain, with a water-filled gap between the two contact surfaces.	INTRO
101	110	interface	site	It involves a GTPase domain surface, which is located at the opposite side of the nucleotide, and an interface in the helical domain, with a water-filled gap between the two contact surfaces.	INTRO
118	132	helical domain	structure_element	It involves a GTPase domain surface, which is located at the opposite side of the nucleotide, and an interface in the helical domain, with a water-filled gap between the two contact surfaces.	INTRO
141	146	water	chemical	It involves a GTPase domain surface, which is located at the opposite side of the nucleotide, and an interface in the helical domain, with a water-filled gap between the two contact surfaces.	INTRO
174	190	contact surfaces	site	It involves a GTPase domain surface, which is located at the opposite side of the nucleotide, and an interface in the helical domain, with a water-filled gap between the two contact surfaces.	INTRO
0	11	Mutagenesis	experimental_method	"Mutagenesis of the contact surfaces suggests that this ""backside"" interface is not required for GTP-dependent oligomerization or cooperative hydrolysis, despite an earlier suggestion to the contrary."	INTRO
19	35	contact surfaces	site	"Mutagenesis of the contact surfaces suggests that this ""backside"" interface is not required for GTP-dependent oligomerization or cooperative hydrolysis, despite an earlier suggestion to the contrary."	INTRO
56	64	backside	site	"Mutagenesis of the contact surfaces suggests that this ""backside"" interface is not required for GTP-dependent oligomerization or cooperative hydrolysis, despite an earlier suggestion to the contrary."	INTRO
66	75	interface	site	"Mutagenesis of the contact surfaces suggests that this ""backside"" interface is not required for GTP-dependent oligomerization or cooperative hydrolysis, despite an earlier suggestion to the contrary."	INTRO
96	99	GTP	chemical	"Mutagenesis of the contact surfaces suggests that this ""backside"" interface is not required for GTP-dependent oligomerization or cooperative hydrolysis, despite an earlier suggestion to the contrary."	INTRO
10	29	biochemical studies	experimental_method	Extensive biochemical studies suggested that GTP-induced oligomerization of Irga6 requires an interface in the GTPase domain across the nucleotide-binding site.	INTRO
45	48	GTP	chemical	Extensive biochemical studies suggested that GTP-induced oligomerization of Irga6 requires an interface in the GTPase domain across the nucleotide-binding site.	INTRO
76	81	Irga6	protein	Extensive biochemical studies suggested that GTP-induced oligomerization of Irga6 requires an interface in the GTPase domain across the nucleotide-binding site.	INTRO
94	103	interface	site	Extensive biochemical studies suggested that GTP-induced oligomerization of Irga6 requires an interface in the GTPase domain across the nucleotide-binding site.	INTRO
111	124	GTPase domain	structure_element	Extensive biochemical studies suggested that GTP-induced oligomerization of Irga6 requires an interface in the GTPase domain across the nucleotide-binding site.	INTRO
136	159	nucleotide-binding site	site	Extensive biochemical studies suggested that GTP-induced oligomerization of Irga6 requires an interface in the GTPase domain across the nucleotide-binding site.	INTRO
7	25	structural studies	experimental_method	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
44	55	G interface	site	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
71	78	dynamin	protein_type	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
108	115	dynamin	protein_type	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
117	120	MxA	protein	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
126	153	guanylate binding protein-1	protein	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
155	160	GBP-1	protein	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
163	171	atlastin	protein_type	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
180	189	bacterial	taxonomy_domain	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
190	211	dynamin-like proteins	protein_type	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
213	217	BDLP	protein_type	Recent structural studies indicated that a 'G interface' is typical of dynamin superfamily members, such as dynamin, MxA, the guanylate binding protein-1 (GBP-1), atlastin and the bacterial dynamin-like proteins (BDLP).	INTRO
48	59	G interface	site	For several of these proteins, formation of the G interface was shown to trigger GTP hydrolysis by inducing rearrangements of catalytic residues in cis.	INTRO
81	84	GTP	chemical	For several of these proteins, formation of the G interface was shown to trigger GTP hydrolysis by inducing rearrangements of catalytic residues in cis.	INTRO
3	10	dynamin	protein_type	In dynamin, the G interface includes residues in the phosphate binding loop, the two switch regions, the 'trans stabilizing loop' and the 'G4 loop'.	INTRO
16	27	G interface	site	In dynamin, the G interface includes residues in the phosphate binding loop, the two switch regions, the 'trans stabilizing loop' and the 'G4 loop'.	INTRO
53	75	phosphate binding loop	structure_element	In dynamin, the G interface includes residues in the phosphate binding loop, the two switch regions, the 'trans stabilizing loop' and the 'G4 loop'.	INTRO
85	99	switch regions	site	In dynamin, the G interface includes residues in the phosphate binding loop, the two switch regions, the 'trans stabilizing loop' and the 'G4 loop'.	INTRO
106	128	trans stabilizing loop	structure_element	In dynamin, the G interface includes residues in the phosphate binding loop, the two switch regions, the 'trans stabilizing loop' and the 'G4 loop'.	INTRO
139	146	G4 loop	structure_element	In dynamin, the G interface includes residues in the phosphate binding loop, the two switch regions, the 'trans stabilizing loop' and the 'G4 loop'.	INTRO
4	9	Irga6	protein	For Irga6, it was demonstrated that besides residues in the switch I and switch II regions, the 3'-OH group of the ribose participates in this interface.	INTRO
60	68	switch I	site	For Irga6, it was demonstrated that besides residues in the switch I and switch II regions, the 3'-OH group of the ribose participates in this interface.	INTRO
73	82	switch II	site	For Irga6, it was demonstrated that besides residues in the switch I and switch II regions, the 3'-OH group of the ribose participates in this interface.	INTRO
143	152	interface	site	For Irga6, it was demonstrated that besides residues in the switch I and switch II regions, the 3'-OH group of the ribose participates in this interface.	INTRO
10	44	signal recognition particle GTPase	protein_type	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
64	72	receptor	protein_type	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
81	84	FfH	protein	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
89	93	FtsY	protein	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
97	105	bacteria	taxonomy_domain	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
145	153	dimerize	oligomeric_state	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
160	173	anti-parallel	protein_state	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
211	217	GTPase	protein_type	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
268	273	Irga6	protein	Since the signal recognition particle GTPase and its homologous receptor (called FfH and FtsY in bacteria) also employ the 3'-OH ribose group to dimerize in an anti-parallel orientation therefore activating its GTPase, an analogous dimerization model was proposed for Irga6.	INTRO
13	30	crystal structure	evidence	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
34	39	Irga6	protein	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
47	58	presence of	protein_state	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
80	83	GTP	chemical	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
93	121	5'-guanylyl imidodiphosphate	chemical	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
123	129	GMPPNP	chemical	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
178	181	apo	protein_state	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
185	194	GDP-bound	protein_state	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
228	243	dimer interface	site	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
264	277	GTPase domain	structure_element	However, the crystal structure of Irga6 in the presence of the non-hydrolyzable GTP analogue 5'-guanylyl imidodiphosphate (GMPPNP) showed only subtle differences relative to the apo or GDP-bound protein and did not reveal a new dimer interface associated with the GTPase domain.	INTRO
5	14	structure	evidence	This structure was obtained by soaking GMPPNP in nucleotide-free crystals of Irga6, an approach which may have interfered with nucleotide-induced domain rearrangements.	INTRO
31	38	soaking	experimental_method	This structure was obtained by soaking GMPPNP in nucleotide-free crystals of Irga6, an approach which may have interfered with nucleotide-induced domain rearrangements.	INTRO
39	45	GMPPNP	chemical	This structure was obtained by soaking GMPPNP in nucleotide-free crystals of Irga6, an approach which may have interfered with nucleotide-induced domain rearrangements.	INTRO
49	64	nucleotide-free	protein_state	This structure was obtained by soaking GMPPNP in nucleotide-free crystals of Irga6, an approach which may have interfered with nucleotide-induced domain rearrangements.	INTRO
65	73	crystals	evidence	This structure was obtained by soaking GMPPNP in nucleotide-free crystals of Irga6, an approach which may have interfered with nucleotide-induced domain rearrangements.	INTRO
77	82	Irga6	protein	This structure was obtained by soaking GMPPNP in nucleotide-free crystals of Irga6, an approach which may have interfered with nucleotide-induced domain rearrangements.	INTRO
41	52	G interface	site	To clarify the dimerization mode via the G interface, we determined the GMPPNP-bound crystal structure of a non-oligomerizing Irga6 variant.	INTRO
57	67	determined	experimental_method	To clarify the dimerization mode via the G interface, we determined the GMPPNP-bound crystal structure of a non-oligomerizing Irga6 variant.	INTRO
72	84	GMPPNP-bound	protein_state	To clarify the dimerization mode via the G interface, we determined the GMPPNP-bound crystal structure of a non-oligomerizing Irga6 variant.	INTRO
85	102	crystal structure	evidence	To clarify the dimerization mode via the G interface, we determined the GMPPNP-bound crystal structure of a non-oligomerizing Irga6 variant.	INTRO
108	125	non-oligomerizing	protein_state	To clarify the dimerization mode via the G interface, we determined the GMPPNP-bound crystal structure of a non-oligomerizing Irga6 variant.	INTRO
126	131	Irga6	protein	To clarify the dimerization mode via the G interface, we determined the GMPPNP-bound crystal structure of a non-oligomerizing Irga6 variant.	INTRO
132	139	variant	protein_state	To clarify the dimerization mode via the G interface, we determined the GMPPNP-bound crystal structure of a non-oligomerizing Irga6 variant.	INTRO
4	13	structure	evidence	The structure revealed that Irga6 can dimerize via the G interface in a parallel head-to-head fashion.	INTRO
28	33	Irga6	protein	The structure revealed that Irga6 can dimerize via the G interface in a parallel head-to-head fashion.	INTRO
38	46	dimerize	oligomeric_state	The structure revealed that Irga6 can dimerize via the G interface in a parallel head-to-head fashion.	INTRO
55	66	G interface	site	The structure revealed that Irga6 can dimerize via the G interface in a parallel head-to-head fashion.	INTRO
72	93	parallel head-to-head	protein_state	The structure revealed that Irga6 can dimerize via the G interface in a parallel head-to-head fashion.	INTRO
24	32	parallel	protein_state	Our data suggest that a parallel dimerization mode may be a unifying feature in all dynamin and septin superfamily proteins.	INTRO
84	91	dynamin	protein_type	Our data suggest that a parallel dimerization mode may be a unifying feature in all dynamin and septin superfamily proteins.	INTRO
96	102	septin	protein_type	Our data suggest that a parallel dimerization mode may be a unifying feature in all dynamin and septin superfamily proteins.	INTRO
32	37	Irga6	protein	"Previous results indicated that Irga6 mutations in a loosely defined surface region (the ""secondary patch""), which is distant from the G-interface and only slightly overlapping with the backside interface (see below), individually reduced GTP-dependent oligomerization."	RESULTS
38	47	mutations	experimental_method	"Previous results indicated that Irga6 mutations in a loosely defined surface region (the ""secondary patch""), which is distant from the G-interface and only slightly overlapping with the backside interface (see below), individually reduced GTP-dependent oligomerization."	RESULTS
69	83	surface region	site	"Previous results indicated that Irga6 mutations in a loosely defined surface region (the ""secondary patch""), which is distant from the G-interface and only slightly overlapping with the backside interface (see below), individually reduced GTP-dependent oligomerization."	RESULTS
90	105	secondary patch	site	"Previous results indicated that Irga6 mutations in a loosely defined surface region (the ""secondary patch""), which is distant from the G-interface and only slightly overlapping with the backside interface (see below), individually reduced GTP-dependent oligomerization."	RESULTS
135	146	G-interface	site	"Previous results indicated that Irga6 mutations in a loosely defined surface region (the ""secondary patch""), which is distant from the G-interface and only slightly overlapping with the backside interface (see below), individually reduced GTP-dependent oligomerization."	RESULTS
186	204	backside interface	site	"Previous results indicated that Irga6 mutations in a loosely defined surface region (the ""secondary patch""), which is distant from the G-interface and only slightly overlapping with the backside interface (see below), individually reduced GTP-dependent oligomerization."	RESULTS
239	242	GTP	chemical	"Previous results indicated that Irga6 mutations in a loosely defined surface region (the ""secondary patch""), which is distant from the G-interface and only slightly overlapping with the backside interface (see below), individually reduced GTP-dependent oligomerization."	RESULTS
2	40	combination of four of these mutations	experimental_method	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
42	46	R31E	mutant	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
48	52	K32E	mutant	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
54	59	K176E	mutant	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
65	70	K246E	mutant	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
84	94	eliminated	protein_state	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
95	98	GTP	chemical	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
161	176	crystallization	experimental_method	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
180	185	Irga6	protein	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
193	204	presence of	protein_state	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
205	211	GMPPNP	chemical	A combination of four of these mutations (R31E, K32E, K176E, and K246E) essentially eliminated GTP-dependent assembly (Additional file 1: Figure S1) and allowed crystallization of Irga6 in the presence of GMPPNP.	RESULTS
0	8	Crystals	evidence	Crystals diffracted to 3.2 Å resolution and displayed one exceptionally long unit cell axis of 1289 Å (Additional file 1: Table S1).	RESULTS
4	13	structure	evidence	The structure was solved by molecular replacement and refined to Rwork/Rfree of 29.7 %/31.7 % (Additional file 1: Table S2).	RESULTS
28	49	molecular replacement	experimental_method	The structure was solved by molecular replacement and refined to Rwork/Rfree of 29.7 %/31.7 % (Additional file 1: Table S2).	RESULTS
65	70	Rwork	evidence	The structure was solved by molecular replacement and refined to Rwork/Rfree of 29.7 %/31.7 % (Additional file 1: Table S2).	RESULTS
71	76	Rfree	evidence	The structure was solved by molecular replacement and refined to Rwork/Rfree of 29.7 %/31.7 % (Additional file 1: Table S2).	RESULTS
36	41	Irga6	protein	The asymmetric unit contained seven Irga6 molecules that were arranged in a helical pattern along the long cell axis (Additional file 1: Figure S2).	RESULTS
0	9	Structure	evidence	Structure of the Irga6 dimer.	FIG
17	22	Irga6	protein	Structure of the Irga6 dimer.	FIG
23	28	dimer	oligomeric_state	Structure of the Irga6 dimer.	FIG
47	52	mouse	taxonomy_domain	a Schematic view of the domain architecture of mouse Irga6.	FIG
53	58	Irga6	protein	a Schematic view of the domain architecture of mouse Irga6.	FIG
36	41	Irga6	protein	b Ribbon-type representation of the Irga6 dimer.	FIG
42	47	dimer	oligomeric_state	b Ribbon-type representation of the Irga6 dimer.	FIG
19	23	Mg2+	chemical	The nucleotide and Mg2+ ion (green) are shown in sphere representation.	FIG
4	17	GTPase domain	structure_element	The GTPase domain dimer is boxed.	FIG
18	23	dimer	oligomeric_state	The GTPase domain dimer is boxed.	FIG
70	83	GTPase domain	structure_element	Secondary structure was numbered according to ref.. c Top view on the GTPase domain dimer.	FIG
84	89	dimer	oligomeric_state	Secondary structure was numbered according to ref.. c Top view on the GTPase domain dimer.	FIG
23	36	contact sites	site	d Magnification of the contact sites.	FIG
2	15	Superposition	experimental_method	e Superposition of different switch I conformations in the asymmetric unit; the same colors as in Additional file 1: Figure S2 are used for the switch I regions of the individual subunits.	FIG
29	37	switch I	site	e Superposition of different switch I conformations in the asymmetric unit; the same colors as in Additional file 1: Figure S2 are used for the switch I regions of the individual subunits.	FIG
144	152	switch I	site	e Superposition of different switch I conformations in the asymmetric unit; the same colors as in Additional file 1: Figure S2 are used for the switch I regions of the individual subunits.	FIG
0	8	Switch I	site	Switch I residues of subunit A (yellow) involved in ribose binding are labelled and shown in stick representation.	FIG
29	30	A	structure_element	Switch I residues of subunit A (yellow) involved in ribose binding are labelled and shown in stick representation.	FIG
0	5	Irga6	protein	Irga6 immunity-related GTPase 6	FIG
6	31	immunity-related GTPase 6	protein	Irga6 immunity-related GTPase 6	FIG
11	18	dynamin	protein_type	Like other dynamin superfamily members, the GTPase domain of Irga6 comprises a canonical GTPase domain fold, with a central β-sheet surrounded by helices on both sides (Fig. 1a-c).	RESULTS
44	57	GTPase domain	structure_element	Like other dynamin superfamily members, the GTPase domain of Irga6 comprises a canonical GTPase domain fold, with a central β-sheet surrounded by helices on both sides (Fig. 1a-c).	RESULTS
61	66	Irga6	protein	Like other dynamin superfamily members, the GTPase domain of Irga6 comprises a canonical GTPase domain fold, with a central β-sheet surrounded by helices on both sides (Fig. 1a-c).	RESULTS
89	102	GTPase domain	structure_element	Like other dynamin superfamily members, the GTPase domain of Irga6 comprises a canonical GTPase domain fold, with a central β-sheet surrounded by helices on both sides (Fig. 1a-c).	RESULTS
124	131	β-sheet	structure_element	Like other dynamin superfamily members, the GTPase domain of Irga6 comprises a canonical GTPase domain fold, with a central β-sheet surrounded by helices on both sides (Fig. 1a-c).	RESULTS
146	153	helices	structure_element	Like other dynamin superfamily members, the GTPase domain of Irga6 comprises a canonical GTPase domain fold, with a central β-sheet surrounded by helices on both sides (Fig. 1a-c).	RESULTS
4	18	helical domain	structure_element	The helical domain is a bipartite structure composed of helices αA-C at the N-terminus and helix αF-L at the C-terminus of the GTPase domain.	RESULTS
56	63	helices	structure_element	The helical domain is a bipartite structure composed of helices αA-C at the N-terminus and helix αF-L at the C-terminus of the GTPase domain.	RESULTS
64	68	αA-C	structure_element	The helical domain is a bipartite structure composed of helices αA-C at the N-terminus and helix αF-L at the C-terminus of the GTPase domain.	RESULTS
91	96	helix	structure_element	The helical domain is a bipartite structure composed of helices αA-C at the N-terminus and helix αF-L at the C-terminus of the GTPase domain.	RESULTS
97	101	αF-L	structure_element	The helical domain is a bipartite structure composed of helices αA-C at the N-terminus and helix αF-L at the C-terminus of the GTPase domain.	RESULTS
127	140	GTPase domain	structure_element	The helical domain is a bipartite structure composed of helices αA-C at the N-terminus and helix αF-L at the C-terminus of the GTPase domain.	RESULTS
89	116	root mean square deviations	evidence	Overall, the seven molecules in the asymmetric unit are very similar to each other, with root mean square deviations (rmsd) ranging from 0.32 – 0.45 Å over all Cα atoms.	RESULTS
118	122	rmsd	evidence	Overall, the seven molecules in the asymmetric unit are very similar to each other, with root mean square deviations (rmsd) ranging from 0.32 – 0.45 Å over all Cα atoms.	RESULTS
4	14	structures	evidence	The structures of the seven molecules also agree well with the previously determined structure of native GMPPNP-bound Irga6 (PDB: 1TQ6; rmsd of 1.00-1.13 Å over all Cα atoms).	RESULTS
85	94	structure	evidence	The structures of the seven molecules also agree well with the previously determined structure of native GMPPNP-bound Irga6 (PDB: 1TQ6; rmsd of 1.00-1.13 Å over all Cα atoms).	RESULTS
98	104	native	protein_state	The structures of the seven molecules also agree well with the previously determined structure of native GMPPNP-bound Irga6 (PDB: 1TQ6; rmsd of 1.00-1.13 Å over all Cα atoms).	RESULTS
105	117	GMPPNP-bound	protein_state	The structures of the seven molecules also agree well with the previously determined structure of native GMPPNP-bound Irga6 (PDB: 1TQ6; rmsd of 1.00-1.13 Å over all Cα atoms).	RESULTS
118	123	Irga6	protein	The structures of the seven molecules also agree well with the previously determined structure of native GMPPNP-bound Irga6 (PDB: 1TQ6; rmsd of 1.00-1.13 Å over all Cα atoms).	RESULTS
136	140	rmsd	evidence	The structures of the seven molecules also agree well with the previously determined structure of native GMPPNP-bound Irga6 (PDB: 1TQ6; rmsd of 1.00-1.13 Å over all Cα atoms).	RESULTS
10	15	Irga6	protein	The seven Irga6 molecules in the asymmetric unit form various higher order contacts in the crystals.	RESULTS
91	99	crystals	evidence	The seven Irga6 molecules in the asymmetric unit form various higher order contacts in the crystals.	RESULTS
42	50	dimerize	oligomeric_state	Within the asymmetric unit, six molecules dimerize via the symmetric backside dimer interface (buried surface area 930 Å2), and the remaining seventh molecule forms the same type of interaction with its symmetry mate of the adjacent asymmetric unit (Additional file 1: Figure S2a, b, Figure S3).	RESULTS
69	93	backside dimer interface	site	Within the asymmetric unit, six molecules dimerize via the symmetric backside dimer interface (buried surface area 930 Å2), and the remaining seventh molecule forms the same type of interaction with its symmetry mate of the adjacent asymmetric unit (Additional file 1: Figure S2a, b, Figure S3).	RESULTS
35	44	mutations	experimental_method	This indicates that the introduced mutations in the secondary patch, from which only Lys176 is part of the backside interface, do, in fact, not prevent this interaction.	RESULTS
52	67	secondary patch	site	This indicates that the introduced mutations in the secondary patch, from which only Lys176 is part of the backside interface, do, in fact, not prevent this interaction.	RESULTS
85	91	Lys176	residue_name_number	This indicates that the introduced mutations in the secondary patch, from which only Lys176 is part of the backside interface, do, in fact, not prevent this interaction.	RESULTS
107	125	backside interface	site	This indicates that the introduced mutations in the secondary patch, from which only Lys176 is part of the backside interface, do, in fact, not prevent this interaction.	RESULTS
8	26	assembly interface	site	Another assembly interface with a buried surface area of 450 Å2, which we call the “tertiary patch”, was formed via two interaction sites in the helical domains (Additional file 1: Figure S2c, d, S3).	RESULTS
84	98	tertiary patch	site	Another assembly interface with a buried surface area of 450 Å2, which we call the “tertiary patch”, was formed via two interaction sites in the helical domains (Additional file 1: Figure S2c, d, S3).	RESULTS
120	137	interaction sites	site	Another assembly interface with a buried surface area of 450 Å2, which we call the “tertiary patch”, was formed via two interaction sites in the helical domains (Additional file 1: Figure S2c, d, S3).	RESULTS
145	160	helical domains	structure_element	Another assembly interface with a buried surface area of 450 Å2, which we call the “tertiary patch”, was formed via two interaction sites in the helical domains (Additional file 1: Figure S2c, d, S3).	RESULTS
8	17	interface	site	In this interface, helices αK from two adjacent molecules form a hydrogen bonding network involving residues 373-376.	RESULTS
19	26	helices	structure_element	In this interface, helices αK from two adjacent molecules form a hydrogen bonding network involving residues 373-376.	RESULTS
27	29	αK	structure_element	In this interface, helices αK from two adjacent molecules form a hydrogen bonding network involving residues 373-376.	RESULTS
65	89	hydrogen bonding network	bond_interaction	In this interface, helices αK from two adjacent molecules form a hydrogen bonding network involving residues 373-376.	RESULTS
109	116	373-376	residue_range	In this interface, helices αK from two adjacent molecules form a hydrogen bonding network involving residues 373-376.	RESULTS
26	33	helices	structure_element	Furthermore, two adjacent helices αA form hydrophobic contacts.	RESULTS
34	36	αA	structure_element	Furthermore, two adjacent helices αA form hydrophobic contacts.	RESULTS
42	62	hydrophobic contacts	bond_interaction	Furthermore, two adjacent helices αA form hydrophobic contacts.	RESULTS
33	48	double mutation	protein_state	It was previously shown that the double mutation L372R/A373R did not prevent GTP-induced assembly, so there is currently no evidence supporting an involvement of this interface in higher-order oligomerization.	RESULTS
49	54	L372R	mutant	It was previously shown that the double mutation L372R/A373R did not prevent GTP-induced assembly, so there is currently no evidence supporting an involvement of this interface in higher-order oligomerization.	RESULTS
55	60	A373R	mutant	It was previously shown that the double mutation L372R/A373R did not prevent GTP-induced assembly, so there is currently no evidence supporting an involvement of this interface in higher-order oligomerization.	RESULTS
77	80	GTP	chemical	It was previously shown that the double mutation L372R/A373R did not prevent GTP-induced assembly, so there is currently no evidence supporting an involvement of this interface in higher-order oligomerization.	RESULTS
167	176	interface	site	It was previously shown that the double mutation L372R/A373R did not prevent GTP-induced assembly, so there is currently no evidence supporting an involvement of this interface in higher-order oligomerization.	RESULTS
21	22	A	structure_element	Strikingly, molecule A of one asymmetric unit assembled with an equivalent molecule of the adjacent asymmetric unit via the G-interface in a symmetric parallel fashion via a 470 Å2 interface.	RESULTS
124	135	G-interface	site	Strikingly, molecule A of one asymmetric unit assembled with an equivalent molecule of the adjacent asymmetric unit via the G-interface in a symmetric parallel fashion via a 470 Å2 interface.	RESULTS
151	159	parallel	protein_state	Strikingly, molecule A of one asymmetric unit assembled with an equivalent molecule of the adjacent asymmetric unit via the G-interface in a symmetric parallel fashion via a 470 Å2 interface.	RESULTS
27	43	butterfly-shaped	protein_state	This assembly results in a butterfly-shaped Irga6 dimer in which the helical domains protrude in parallel orientations (Fig. 1b, Additional file 1: Figure S3).	RESULTS
44	49	Irga6	protein	This assembly results in a butterfly-shaped Irga6 dimer in which the helical domains protrude in parallel orientations (Fig. 1b, Additional file 1: Figure S3).	RESULTS
50	55	dimer	oligomeric_state	This assembly results in a butterfly-shaped Irga6 dimer in which the helical domains protrude in parallel orientations (Fig. 1b, Additional file 1: Figure S3).	RESULTS
69	84	helical domains	structure_element	This assembly results in a butterfly-shaped Irga6 dimer in which the helical domains protrude in parallel orientations (Fig. 1b, Additional file 1: Figure S3).	RESULTS
97	105	parallel	protein_state	This assembly results in a butterfly-shaped Irga6 dimer in which the helical domains protrude in parallel orientations (Fig. 1b, Additional file 1: Figure S3).	RESULTS
84	95	G interface	site	In contrast, the other six molecules in the asymmetric unit do not assemble via the G interface.	RESULTS
4	15	G interface	site	The G interface in molecule A can be subdivided into three distinct contact sites (Fig. 1c, d).	RESULTS
68	81	contact sites	site	The G interface in molecule A can be subdivided into three distinct contact sites (Fig. 1c, d).	RESULTS
0	14	Contact site I	site	Contact site I is formed between R159 and K161 in the trans stabilizing loops, and S132 in the switch II regions of the opposing molecules.	RESULTS
33	37	R159	residue_name_number	Contact site I is formed between R159 and K161 in the trans stabilizing loops, and S132 in the switch II regions of the opposing molecules.	RESULTS
42	46	K161	residue_name_number	Contact site I is formed between R159 and K161 in the trans stabilizing loops, and S132 in the switch II regions of the opposing molecules.	RESULTS
54	77	trans stabilizing loops	structure_element	Contact site I is formed between R159 and K161 in the trans stabilizing loops, and S132 in the switch II regions of the opposing molecules.	RESULTS
83	87	S132	residue_name_number	Contact site I is formed between R159 and K161 in the trans stabilizing loops, and S132 in the switch II regions of the opposing molecules.	RESULTS
95	104	switch II	site	Contact site I is formed between R159 and K161 in the trans stabilizing loops, and S132 in the switch II regions of the opposing molecules.	RESULTS
0	15	Contact site II	site	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
25	59	polar and hydrophobic interactions	bond_interaction	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
70	78	switch I	site	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
80	84	V104	residue_name_number	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
86	90	V107	residue_name_number	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
99	104	helix	structure_element	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
119	144	guanine specificity motif	structure_element	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
146	154	G4 helix	structure_element	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
156	160	K184	residue_name_number	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
165	169	S187	residue_name_number	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
179	201	trans stabilizing loop	structure_element	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
203	207	T158	residue_name_number	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
225	238	GTPase domain	structure_element	Contact site II features polar and hydrophobic interactions formed by switch I (V104, V107) with a helix following the guanine specificity motif (G4 helix, K184 and S187) and the trans stabilizing loop (T158) of the opposing GTPase domain.	RESULTS
3	19	contact site III	site	In contact site III, G103 of switch I interacts via its main chain nitrogen with the exocyclic 2’-OH and 3’-OH groups of the opposing ribose in trans, whereas the two opposing exocyclic 3’-OH group of the ribose form hydrogen bonds with each other.	RESULTS
21	25	G103	residue_name_number	In contact site III, G103 of switch I interacts via its main chain nitrogen with the exocyclic 2’-OH and 3’-OH groups of the opposing ribose in trans, whereas the two opposing exocyclic 3’-OH group of the ribose form hydrogen bonds with each other.	RESULTS
29	37	switch I	site	In contact site III, G103 of switch I interacts via its main chain nitrogen with the exocyclic 2’-OH and 3’-OH groups of the opposing ribose in trans, whereas the two opposing exocyclic 3’-OH group of the ribose form hydrogen bonds with each other.	RESULTS
134	140	ribose	chemical	In contact site III, G103 of switch I interacts via its main chain nitrogen with the exocyclic 2’-OH and 3’-OH groups of the opposing ribose in trans, whereas the two opposing exocyclic 3’-OH group of the ribose form hydrogen bonds with each other.	RESULTS
205	211	ribose	chemical	In contact site III, G103 of switch I interacts via its main chain nitrogen with the exocyclic 2’-OH and 3’-OH groups of the opposing ribose in trans, whereas the two opposing exocyclic 3’-OH group of the ribose form hydrogen bonds with each other.	RESULTS
217	231	hydrogen bonds	bond_interaction	In contact site III, G103 of switch I interacts via its main chain nitrogen with the exocyclic 2’-OH and 3’-OH groups of the opposing ribose in trans, whereas the two opposing exocyclic 3’-OH group of the ribose form hydrogen bonds with each other.	RESULTS
8	14	ribose	chemical	Via the ribose contact, switch I is pulled towards the opposing nucleotide (Fig. 1e).	RESULTS
24	32	switch I	site	Via the ribose contact, switch I is pulled towards the opposing nucleotide (Fig. 1e).	RESULTS
64	74	nucleotide	chemical	Via the ribose contact, switch I is pulled towards the opposing nucleotide (Fig. 1e).	RESULTS
9	13	E106	residue_name_number	In turn, E106 of switch I reorients towards the nucleotide and now participates in the coordination of the Mg2+ ion (Fig. 1e, Additional file 1: Figure S4).	RESULTS
17	25	switch I	site	In turn, E106 of switch I reorients towards the nucleotide and now participates in the coordination of the Mg2+ ion (Fig. 1e, Additional file 1: Figure S4).	RESULTS
48	58	nucleotide	chemical	In turn, E106 of switch I reorients towards the nucleotide and now participates in the coordination of the Mg2+ ion (Fig. 1e, Additional file 1: Figure S4).	RESULTS
87	102	coordination of	bond_interaction	In turn, E106 of switch I reorients towards the nucleotide and now participates in the coordination of the Mg2+ ion (Fig. 1e, Additional file 1: Figure S4).	RESULTS
107	111	Mg2+	chemical	In turn, E106 of switch I reorients towards the nucleotide and now participates in the coordination of the Mg2+ ion (Fig. 1e, Additional file 1: Figure S4).	RESULTS
0	4	E106	residue_name_number	E106 was previously shown to be essential for catalysis, and the observed interactions in contact site III explain how dimerization via the ribose is directly coupled to the activation of GTP hydrolysis.	RESULTS
90	106	contact site III	site	E106 was previously shown to be essential for catalysis, and the observed interactions in contact site III explain how dimerization via the ribose is directly coupled to the activation of GTP hydrolysis.	RESULTS
140	146	ribose	chemical	E106 was previously shown to be essential for catalysis, and the observed interactions in contact site III explain how dimerization via the ribose is directly coupled to the activation of GTP hydrolysis.	RESULTS
188	191	GTP	chemical	E106 was previously shown to be essential for catalysis, and the observed interactions in contact site III explain how dimerization via the ribose is directly coupled to the activation of GTP hydrolysis.	RESULTS
4	15	G interface	site	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
111	114	E77	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
116	120	G103	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
122	126	E106	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
128	132	S132	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
134	138	R159	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
140	144	K161	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
146	150	K162	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
152	156	D164	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
158	162	N191	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
168	172	K196	residue_name_number	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
221	224	GTP	chemical	The G interface is in full agreement with previously published biochemical data that indicate crucial roles of E77, G103, E106, S132, R159, K161, K162, D164, N191, and K196 for oligomerization and oligomerization-induced GTP hydrolysis.	RESULTS
56	60	G103	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
62	66	S132	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
68	72	R159	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
78	82	K161	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
117	126	interface	site	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
128	131	E77	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
133	137	E106	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
139	143	K162	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
145	149	D164	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
155	159	N191	residue_name_number	All of these residues directly participate in contacts (G103, S132, R159, and K161) or are in direct vicinity to the interface (E77, E106, K162, D164, and N191).	RESULTS
9	12	E77	residue_name_number	Residues E77, K162, and D164 appear to orient the trans stabilizing loop which is involved in interface formation in contact site II.	RESULTS
14	18	K162	residue_name_number	Residues E77, K162, and D164 appear to orient the trans stabilizing loop which is involved in interface formation in contact site II.	RESULTS
24	28	D164	residue_name_number	Residues E77, K162, and D164 appear to orient the trans stabilizing loop which is involved in interface formation in contact site II.	RESULTS
50	72	trans stabilizing loop	structure_element	Residues E77, K162, and D164 appear to orient the trans stabilizing loop which is involved in interface formation in contact site II.	RESULTS
94	103	interface	site	Residues E77, K162, and D164 appear to orient the trans stabilizing loop which is involved in interface formation in contact site II.	RESULTS
117	132	contact site II	site	Residues E77, K162, and D164 appear to orient the trans stabilizing loop which is involved in interface formation in contact site II.	RESULTS
27	40	anti-parallel	protein_state	In the earlier model of an anti-parallel G interface, it was not possible to position the side chain of R159 to avoid steric conflict.	RESULTS
41	52	G interface	site	In the earlier model of an anti-parallel G interface, it was not possible to position the side chain of R159 to avoid steric conflict.	RESULTS
104	108	R159	residue_name_number	In the earlier model of an anti-parallel G interface, it was not possible to position the side chain of R159 to avoid steric conflict.	RESULTS
15	24	structure	evidence	In the present structure, the side-chain of R159 projects laterally along the G interface and, therefore, does not cause a steric conflict.	RESULTS
44	48	R159	residue_name_number	In the present structure, the side-chain of R159 projects laterally along the G interface and, therefore, does not cause a steric conflict.	RESULTS
78	89	G interface	site	In the present structure, the side-chain of R159 projects laterally along the G interface and, therefore, does not cause a steric conflict.	RESULTS
38	49	G interface	site	A conserved dimerization mode via the G interface in dynamin and septin GTPases.	FIG
53	60	dynamin	protein_type	A conserved dimerization mode via the G interface in dynamin and septin GTPases.	FIG
65	79	septin GTPases	protein_type	A conserved dimerization mode via the G interface in dynamin and septin GTPases.	FIG
32	40	parallel	protein_state	The overall architecture of the parallel GTPase domain dimer of Irga6 is related to that of other dynamin and septin superfamily proteins.	FIG
41	54	GTPase domain	structure_element	The overall architecture of the parallel GTPase domain dimer of Irga6 is related to that of other dynamin and septin superfamily proteins.	FIG
55	60	dimer	oligomeric_state	The overall architecture of the parallel GTPase domain dimer of Irga6 is related to that of other dynamin and septin superfamily proteins.	FIG
64	69	Irga6	protein	The overall architecture of the parallel GTPase domain dimer of Irga6 is related to that of other dynamin and septin superfamily proteins.	FIG
98	105	dynamin	protein_type	The overall architecture of the parallel GTPase domain dimer of Irga6 is related to that of other dynamin and septin superfamily proteins.	FIG
110	116	septin	protein_type	The overall architecture of the parallel GTPase domain dimer of Irga6 is related to that of other dynamin and septin superfamily proteins.	FIG
14	24	structures	evidence	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
97	111	GTPase domains	structure_element	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
119	131	GMPPNP-bound	protein_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
132	137	Irga6	protein	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
138	143	dimer	oligomeric_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
168	177	dynamin 1	protein	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
178	192	GTPase-minimal	structure_element	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
225	234	GDP-bound	protein_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
235	245	atlastin 1	protein	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
246	251	dimer	oligomeric_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
270	285	GDP-AlF3- bound	protein_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
286	290	GBP1	protein	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
291	304	GTPase domain	structure_element	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
305	310	dimer	oligomeric_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
329	333	BDLP	protein_type	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
334	339	dimer	oligomeric_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
340	348	bound to	protein_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
349	352	GDP	chemical	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
374	383	GTP-bound	protein_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
384	390	GIMAP2	protein	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
391	396	dimer	oligomeric_state	The following structures are shown in cylinder representations, in similar orientations of their GTPase domains: a the GMPPNP-bound Irga6 dimer, b the GDP-AlF4 --bound dynamin 1 GTPase-minimal BSE construct [pdb 2X2E], c the GDP-bound atlastin 1 dimer [pdb 3Q5E], d the GDP-AlF3- bound GBP1 GTPase domain dimer [pdb 2B92], e the BDLP dimer bound to GDP [pdb 2J68] and f the GTP-bound GIMAP2 dimer [pdb 2XTN].	FIG
4	18	GTPase domains	structure_element	The GTPase domains of the left molecules are shown in orange, helical domains or extensions in blue.	FIG
62	77	helical domains	structure_element	The GTPase domains of the left molecules are shown in orange, helical domains or extensions in blue.	FIG
12	16	Mg2+	chemical	Nucleotide, Mg2+ (green) and AlF4 - are shown in sphere representation, the buried interface sizes per molecule are indicated on the right.	FIG
83	92	interface	site	Nucleotide, Mg2+ (green) and AlF4 - are shown in sphere representation, the buried interface sizes per molecule are indicated on the right.	FIG
0	5	Irga6	protein	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
6	31	immunity-related GTPase 6	protein	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
33	39	GMPPNP	chemical	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
40	68	5'-guanylyl imidodiphosphate	chemical	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
70	73	GTP	chemical	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
74	96	guanosine-triphosphate	chemical	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
98	102	BDLP	protein_type	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
103	112	bacterial	taxonomy_domain	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
113	133	dynamin like protein	protein_type	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
135	141	GIMAP2	protein	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
143	182	GTPase of immunity associated protein 2	protein	Irga6 immunity-related GTPase 6, GMPPNP 5'-guanylyl imidodiphosphate, GTP guanosine-triphosphate, BDLP bacterial dynamin like protein, GIMAP2, GTPase of immunity associated protein 2	FIG
50	61	G interface	site	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
65	70	Irga6	protein	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
126	133	dynamin	protein_type	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
163	170	dynamin	protein_type	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
187	195	atlastin	protein_type	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
211	216	GBP-1	protein	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
233	237	BDLP	protein_type	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
260	314	septin-related GTPase of immunity associated protein 2	protein	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
316	322	GIMAP2	protein	The buried surface area per molecule (BSA) of the G interface in Irga6 is relatively small (470 Å2) compared to that of other dynamin superfamily members, such as dynamin (BSA: 1400 Å2), atlastin (BSA: 820 Å2), GBP-1 (BSA: 2060 Å2), BDLP (BSA: 2300 Å2) or the septin-related GTPase of immunity associated protein 2 (GIMAP2) (BSA: 590 Å2) (Fig. 2).	RESULTS
42	56	GTPase domains	structure_element	However, the relative orientations of the GTPase domains in these dimers are strikingly similar, and the same elements, such as switch I, switch II, the trans activating and G4 loops are involved in the parallel dimerization mode in all of these GTPase families.	RESULTS
66	72	dimers	oligomeric_state	However, the relative orientations of the GTPase domains in these dimers are strikingly similar, and the same elements, such as switch I, switch II, the trans activating and G4 loops are involved in the parallel dimerization mode in all of these GTPase families.	RESULTS
128	136	switch I	site	However, the relative orientations of the GTPase domains in these dimers are strikingly similar, and the same elements, such as switch I, switch II, the trans activating and G4 loops are involved in the parallel dimerization mode in all of these GTPase families.	RESULTS
138	147	switch II	site	However, the relative orientations of the GTPase domains in these dimers are strikingly similar, and the same elements, such as switch I, switch II, the trans activating and G4 loops are involved in the parallel dimerization mode in all of these GTPase families.	RESULTS
153	182	trans activating and G4 loops	structure_element	However, the relative orientations of the GTPase domains in these dimers are strikingly similar, and the same elements, such as switch I, switch II, the trans activating and G4 loops are involved in the parallel dimerization mode in all of these GTPase families.	RESULTS
203	211	parallel	protein_state	However, the relative orientations of the GTPase domains in these dimers are strikingly similar, and the same elements, such as switch I, switch II, the trans activating and G4 loops are involved in the parallel dimerization mode in all of these GTPase families.	RESULTS
246	252	GTPase	protein_type	However, the relative orientations of the GTPase domains in these dimers are strikingly similar, and the same elements, such as switch I, switch II, the trans activating and G4 loops are involved in the parallel dimerization mode in all of these GTPase families.	RESULTS
0	3	IRG	protein_type	IRG proteins are crucial mediators of the innate immune response in mice against a specific subset of intracellular pathogens, all of which enter the cell to form a membrane-bounded vacuole without engagement of the phagocytic machinery.	DISCUSS
68	72	mice	taxonomy_domain	IRG proteins are crucial mediators of the innate immune response in mice against a specific subset of intracellular pathogens, all of which enter the cell to form a membrane-bounded vacuole without engagement of the phagocytic machinery.	DISCUSS
18	25	dynamin	protein_type	As members of the dynamin superfamily, IRGs oligomerize at cellular membranes in response to GTP binding.	DISCUSS
39	43	IRGs	protein_type	As members of the dynamin superfamily, IRGs oligomerize at cellular membranes in response to GTP binding.	DISCUSS
93	96	GTP	chemical	As members of the dynamin superfamily, IRGs oligomerize at cellular membranes in response to GTP binding.	DISCUSS
44	47	GTP	chemical	Oligomerization and oligomerization-induced GTP hydrolysis are thought to induce membrane remodeling events ultimately leading to disruption of the PVM.	DISCUSS
7	42	structural and mechanistic analyses	experimental_method	Recent structural and mechanistic analyses have begun to unravel the molecular basis for the membrane-remodeling activity and mechano-chemical function of some members (reviewed in).	DISCUSS
17	24	dynamin	protein_type	For example, for dynamin and atlastin, it was shown that GTP binding and/or hydrolysis leads to dimerization of the GTPase domains and to the reorientation of the adjacent helical domains.	DISCUSS
29	37	atlastin	protein_type	For example, for dynamin and atlastin, it was shown that GTP binding and/or hydrolysis leads to dimerization of the GTPase domains and to the reorientation of the adjacent helical domains.	DISCUSS
57	60	GTP	chemical	For example, for dynamin and atlastin, it was shown that GTP binding and/or hydrolysis leads to dimerization of the GTPase domains and to the reorientation of the adjacent helical domains.	DISCUSS
116	130	GTPase domains	structure_element	For example, for dynamin and atlastin, it was shown that GTP binding and/or hydrolysis leads to dimerization of the GTPase domains and to the reorientation of the adjacent helical domains.	DISCUSS
172	187	helical domains	structure_element	For example, for dynamin and atlastin, it was shown that GTP binding and/or hydrolysis leads to dimerization of the GTPase domains and to the reorientation of the adjacent helical domains.	DISCUSS
19	26	dynamin	protein_type	However, for other dynamin superfamily members such as IRGs, the molecular basis for GTP hydrolysis and the exact role of the mechano-chemical function are still unclear.	DISCUSS
55	59	IRGs	protein_type	However, for other dynamin superfamily members such as IRGs, the molecular basis for GTP hydrolysis and the exact role of the mechano-chemical function are still unclear.	DISCUSS
85	88	GTP	chemical	However, for other dynamin superfamily members such as IRGs, the molecular basis for GTP hydrolysis and the exact role of the mechano-chemical function are still unclear.	DISCUSS
4	23	structural analysis	experimental_method	Our structural analysis of an oligomerization- and GTPase-defective Irga6 mutant indicates that Irga6 dimerizes via the G interface in a parallel orientation.	DISCUSS
30	67	oligomerization- and GTPase-defective	protein_state	Our structural analysis of an oligomerization- and GTPase-defective Irga6 mutant indicates that Irga6 dimerizes via the G interface in a parallel orientation.	DISCUSS
68	73	Irga6	protein	Our structural analysis of an oligomerization- and GTPase-defective Irga6 mutant indicates that Irga6 dimerizes via the G interface in a parallel orientation.	DISCUSS
74	80	mutant	protein_state	Our structural analysis of an oligomerization- and GTPase-defective Irga6 mutant indicates that Irga6 dimerizes via the G interface in a parallel orientation.	DISCUSS
96	101	Irga6	protein	Our structural analysis of an oligomerization- and GTPase-defective Irga6 mutant indicates that Irga6 dimerizes via the G interface in a parallel orientation.	DISCUSS
102	111	dimerizes	oligomeric_state	Our structural analysis of an oligomerization- and GTPase-defective Irga6 mutant indicates that Irga6 dimerizes via the G interface in a parallel orientation.	DISCUSS
120	131	G interface	site	Our structural analysis of an oligomerization- and GTPase-defective Irga6 mutant indicates that Irga6 dimerizes via the G interface in a parallel orientation.	DISCUSS
137	145	parallel	protein_state	Our structural analysis of an oligomerization- and GTPase-defective Irga6 mutant indicates that Irga6 dimerizes via the G interface in a parallel orientation.	DISCUSS
22	27	Irga6	protein	Only one of the seven Irga6 molecules in the asymmetric unit formed this contact pointing to a low affinity interaction via the G interface, which is in agreement with its small size.	DISCUSS
128	139	G interface	site	Only one of the seven Irga6 molecules in the asymmetric unit formed this contact pointing to a low affinity interaction via the G interface, which is in agreement with its small size.	DISCUSS
7	15	crystals	evidence	In the crystals, dimerization via the G interface is promoted by the high protein concentrations which may mimic a situation when Irga6 oligomerizes on a membrane surface.	DISCUSS
38	49	G interface	site	In the crystals, dimerization via the G interface is promoted by the high protein concentrations which may mimic a situation when Irga6 oligomerizes on a membrane surface.	DISCUSS
130	135	Irga6	protein	In the crystals, dimerization via the G interface is promoted by the high protein concentrations which may mimic a situation when Irga6 oligomerizes on a membrane surface.	DISCUSS
90	93	GTP	chemical	Such a low affinity interaction mode may allow reversibility of oligomerization following GTP hydrolysis.	DISCUSS
21	32	G interface	site	Similar low affinity G interface interactions were reported for dynamin and MxA.	DISCUSS
64	71	dynamin	protein_type	Similar low affinity G interface interactions were reported for dynamin and MxA.	DISCUSS
76	79	MxA	protein	Similar low affinity G interface interactions were reported for dynamin and MxA.	DISCUSS
75	88	anti-parallel	protein_state	The dimerization mode is strikingly different from the previously proposed anti-parallel model that was based on the crystal structure of the signal recognition particle GTPase, SRP54 and its homologous receptor.	DISCUSS
117	134	crystal structure	evidence	The dimerization mode is strikingly different from the previously proposed anti-parallel model that was based on the crystal structure of the signal recognition particle GTPase, SRP54 and its homologous receptor.	DISCUSS
142	176	signal recognition particle GTPase	protein_type	The dimerization mode is strikingly different from the previously proposed anti-parallel model that was based on the crystal structure of the signal recognition particle GTPase, SRP54 and its homologous receptor.	DISCUSS
178	183	SRP54	protein	The dimerization mode is strikingly different from the previously proposed anti-parallel model that was based on the crystal structure of the signal recognition particle GTPase, SRP54 and its homologous receptor.	DISCUSS
13	30	G dimer interface	site	However, the G dimer interface is reminiscent of the GTPase domain dimers observed for several other dynamin superfamily members, such as dynamin, GBP1, atlastin, and BDLP.	DISCUSS
53	66	GTPase domain	structure_element	However, the G dimer interface is reminiscent of the GTPase domain dimers observed for several other dynamin superfamily members, such as dynamin, GBP1, atlastin, and BDLP.	DISCUSS
67	73	dimers	oligomeric_state	However, the G dimer interface is reminiscent of the GTPase domain dimers observed for several other dynamin superfamily members, such as dynamin, GBP1, atlastin, and BDLP.	DISCUSS
101	108	dynamin	protein_type	However, the G dimer interface is reminiscent of the GTPase domain dimers observed for several other dynamin superfamily members, such as dynamin, GBP1, atlastin, and BDLP.	DISCUSS
138	145	dynamin	protein_type	However, the G dimer interface is reminiscent of the GTPase domain dimers observed for several other dynamin superfamily members, such as dynamin, GBP1, atlastin, and BDLP.	DISCUSS
147	151	GBP1	protein	However, the G dimer interface is reminiscent of the GTPase domain dimers observed for several other dynamin superfamily members, such as dynamin, GBP1, atlastin, and BDLP.	DISCUSS
153	161	atlastin	protein_type	However, the G dimer interface is reminiscent of the GTPase domain dimers observed for several other dynamin superfamily members, such as dynamin, GBP1, atlastin, and BDLP.	DISCUSS
167	171	BDLP	protein_type	However, the G dimer interface is reminiscent of the GTPase domain dimers observed for several other dynamin superfamily members, such as dynamin, GBP1, atlastin, and BDLP.	DISCUSS
27	33	septin	protein_type	It was recently shown that septin and septin-related GTPases, such as the Tocs GTPases or GTPases of immunity related proteins (GIMAPs), also employ a GTP-dependent parallel dimerization mode.	DISCUSS
38	60	septin-related GTPases	protein_type	It was recently shown that septin and septin-related GTPases, such as the Tocs GTPases or GTPases of immunity related proteins (GIMAPs), also employ a GTP-dependent parallel dimerization mode.	DISCUSS
74	86	Tocs GTPases	protein_type	It was recently shown that septin and septin-related GTPases, such as the Tocs GTPases or GTPases of immunity related proteins (GIMAPs), also employ a GTP-dependent parallel dimerization mode.	DISCUSS
90	126	GTPases of immunity related proteins	protein_type	It was recently shown that septin and septin-related GTPases, such as the Tocs GTPases or GTPases of immunity related proteins (GIMAPs), also employ a GTP-dependent parallel dimerization mode.	DISCUSS
128	134	GIMAPs	protein_type	It was recently shown that septin and septin-related GTPases, such as the Tocs GTPases or GTPases of immunity related proteins (GIMAPs), also employ a GTP-dependent parallel dimerization mode.	DISCUSS
151	154	GTP	chemical	It was recently shown that septin and septin-related GTPases, such as the Tocs GTPases or GTPases of immunity related proteins (GIMAPs), also employ a GTP-dependent parallel dimerization mode.	DISCUSS
165	173	parallel	protein_state	It was recently shown that septin and septin-related GTPases, such as the Tocs GTPases or GTPases of immunity related proteins (GIMAPs), also employ a GTP-dependent parallel dimerization mode.	DISCUSS
9	45	phylogenetic and structural analysis	experimental_method	Based on phylogenetic and structural analysis, these observations suggest that dynamin and septin superfamilies are derived from a common ancestral membrane-associated GTPase that featured a GTP-dependent parallel dimerization mode.	DISCUSS
79	86	dynamin	protein_type	Based on phylogenetic and structural analysis, these observations suggest that dynamin and septin superfamilies are derived from a common ancestral membrane-associated GTPase that featured a GTP-dependent parallel dimerization mode.	DISCUSS
91	97	septin	protein_type	Based on phylogenetic and structural analysis, these observations suggest that dynamin and septin superfamilies are derived from a common ancestral membrane-associated GTPase that featured a GTP-dependent parallel dimerization mode.	DISCUSS
148	174	membrane-associated GTPase	protein_type	Based on phylogenetic and structural analysis, these observations suggest that dynamin and septin superfamilies are derived from a common ancestral membrane-associated GTPase that featured a GTP-dependent parallel dimerization mode.	DISCUSS
191	194	GTP	chemical	Based on phylogenetic and structural analysis, these observations suggest that dynamin and septin superfamilies are derived from a common ancestral membrane-associated GTPase that featured a GTP-dependent parallel dimerization mode.	DISCUSS
205	213	parallel	protein_state	Based on phylogenetic and structural analysis, these observations suggest that dynamin and septin superfamilies are derived from a common ancestral membrane-associated GTPase that featured a GTP-dependent parallel dimerization mode.	DISCUSS
41	45	IRGs	protein_type	Importantly, our analysis indicates that IRGs are not outliers, but bona-fide representatives of the dynamin superfamily.	DISCUSS
101	108	dynamin	protein_type	Importantly, our analysis indicates that IRGs are not outliers, but bona-fide representatives of the dynamin superfamily.	DISCUSS
52	58	septin	protein_type	Whereas the overall dimerization mode is similar in septin and dynamin GTPases, family-specific differences in the G interface and the oligomerization interfaces exist.	DISCUSS
63	78	dynamin GTPases	protein_type	Whereas the overall dimerization mode is similar in septin and dynamin GTPases, family-specific differences in the G interface and the oligomerization interfaces exist.	DISCUSS
115	126	G interface	site	Whereas the overall dimerization mode is similar in septin and dynamin GTPases, family-specific differences in the G interface and the oligomerization interfaces exist.	DISCUSS
135	161	oligomerization interfaces	site	Whereas the overall dimerization mode is similar in septin and dynamin GTPases, family-specific differences in the G interface and the oligomerization interfaces exist.	DISCUSS
63	69	ribose	chemical	For example, the involvement of the 2’ and 3’-OH groups of the ribose in the dimerization interface of Irga6 has not been observed for other dynamin and septin superfamily members.	DISCUSS
77	99	dimerization interface	site	For example, the involvement of the 2’ and 3’-OH groups of the ribose in the dimerization interface of Irga6 has not been observed for other dynamin and septin superfamily members.	DISCUSS
103	108	Irga6	protein	For example, the involvement of the 2’ and 3’-OH groups of the ribose in the dimerization interface of Irga6 has not been observed for other dynamin and septin superfamily members.	DISCUSS
141	148	dynamin	protein_type	For example, the involvement of the 2’ and 3’-OH groups of the ribose in the dimerization interface of Irga6 has not been observed for other dynamin and septin superfamily members.	DISCUSS
153	159	septin	protein_type	For example, the involvement of the 2’ and 3’-OH groups of the ribose in the dimerization interface of Irga6 has not been observed for other dynamin and septin superfamily members.	DISCUSS
50	55	Irga6	protein	The surface-exposed location of the ribose in the Irga6 structure, with a wide-open nucleotide-binding pocket, facilitates its engagement in the dimerization interface.	DISCUSS
56	65	structure	evidence	The surface-exposed location of the ribose in the Irga6 structure, with a wide-open nucleotide-binding pocket, facilitates its engagement in the dimerization interface.	DISCUSS
74	83	wide-open	protein_state	The surface-exposed location of the ribose in the Irga6 structure, with a wide-open nucleotide-binding pocket, facilitates its engagement in the dimerization interface.	DISCUSS
84	109	nucleotide-binding pocket	site	The surface-exposed location of the ribose in the Irga6 structure, with a wide-open nucleotide-binding pocket, facilitates its engagement in the dimerization interface.	DISCUSS
145	167	dimerization interface	site	The surface-exposed location of the ribose in the Irga6 structure, with a wide-open nucleotide-binding pocket, facilitates its engagement in the dimerization interface.	DISCUSS
43	46	GTP	chemical	This contact, in turn, appears to activate GTP hydrolysis by inducing rearrangements in switch I and the positioning of the catalytic E106.	DISCUSS
88	96	switch I	site	This contact, in turn, appears to activate GTP hydrolysis by inducing rearrangements in switch I and the positioning of the catalytic E106.	DISCUSS
124	133	catalytic	protein_state	This contact, in turn, appears to activate GTP hydrolysis by inducing rearrangements in switch I and the positioning of the catalytic E106.	DISCUSS
134	138	E106	residue_name_number	This contact, in turn, appears to activate GTP hydrolysis by inducing rearrangements in switch I and the positioning of the catalytic E106.	DISCUSS
23	27	GBP1	protein	During dimerization of GBP1, an arginine finger from the P loop reorients towards the nucleotide in cis to trigger GTP hydrolysis.	DISCUSS
32	47	arginine finger	structure_element	During dimerization of GBP1, an arginine finger from the P loop reorients towards the nucleotide in cis to trigger GTP hydrolysis.	DISCUSS
57	63	P loop	structure_element	During dimerization of GBP1, an arginine finger from the P loop reorients towards the nucleotide in cis to trigger GTP hydrolysis.	DISCUSS
86	96	nucleotide	chemical	During dimerization of GBP1, an arginine finger from the P loop reorients towards the nucleotide in cis to trigger GTP hydrolysis.	DISCUSS
115	118	GTP	chemical	During dimerization of GBP1, an arginine finger from the P loop reorients towards the nucleotide in cis to trigger GTP hydrolysis.	DISCUSS
3	10	dynamin	protein_type	In dynamin, the corresponding serine residue coordinates a sodium ion that is crucial for GTP hydrolysis.	DISCUSS
30	36	serine	residue_name	In dynamin, the corresponding serine residue coordinates a sodium ion that is crucial for GTP hydrolysis.	DISCUSS
59	65	sodium	chemical	In dynamin, the corresponding serine residue coordinates a sodium ion that is crucial for GTP hydrolysis.	DISCUSS
90	93	GTP	chemical	In dynamin, the corresponding serine residue coordinates a sodium ion that is crucial for GTP hydrolysis.	DISCUSS
0	5	Irga6	protein	Irga6 bears Gly79 at this position, which in the dimerizing molecule A appears to approach the bridging imido group of GMPPNP via a main chain hydrogen bond.	DISCUSS
12	17	Gly79	residue_name_number	Irga6 bears Gly79 at this position, which in the dimerizing molecule A appears to approach the bridging imido group of GMPPNP via a main chain hydrogen bond.	DISCUSS
49	59	dimerizing	oligomeric_state	Irga6 bears Gly79 at this position, which in the dimerizing molecule A appears to approach the bridging imido group of GMPPNP via a main chain hydrogen bond.	DISCUSS
69	70	A	structure_element	Irga6 bears Gly79 at this position, which in the dimerizing molecule A appears to approach the bridging imido group of GMPPNP via a main chain hydrogen bond.	DISCUSS
119	125	GMPPNP	chemical	Irga6 bears Gly79 at this position, which in the dimerizing molecule A appears to approach the bridging imido group of GMPPNP via a main chain hydrogen bond.	DISCUSS
143	156	hydrogen bond	bond_interaction	Irga6 bears Gly79 at this position, which in the dimerizing molecule A appears to approach the bridging imido group of GMPPNP via a main chain hydrogen bond.	DISCUSS
18	28	structures	evidence	Higher resolution structures of the Irga6 dimer in the presence of a transition state analogue are required to show whether Gly79 directly participates in GTP hydrolysis or whether it may also position a catalytic cation.	DISCUSS
36	41	Irga6	protein	Higher resolution structures of the Irga6 dimer in the presence of a transition state analogue are required to show whether Gly79 directly participates in GTP hydrolysis or whether it may also position a catalytic cation.	DISCUSS
42	47	dimer	oligomeric_state	Higher resolution structures of the Irga6 dimer in the presence of a transition state analogue are required to show whether Gly79 directly participates in GTP hydrolysis or whether it may also position a catalytic cation.	DISCUSS
55	66	presence of	protein_state	Higher resolution structures of the Irga6 dimer in the presence of a transition state analogue are required to show whether Gly79 directly participates in GTP hydrolysis or whether it may also position a catalytic cation.	DISCUSS
124	129	Gly79	residue_name_number	Higher resolution structures of the Irga6 dimer in the presence of a transition state analogue are required to show whether Gly79 directly participates in GTP hydrolysis or whether it may also position a catalytic cation.	DISCUSS
155	158	GTP	chemical	Higher resolution structures of the Irga6 dimer in the presence of a transition state analogue are required to show whether Gly79 directly participates in GTP hydrolysis or whether it may also position a catalytic cation.	DISCUSS
3	10	dynamin	protein_type	In dynamin, further assembly sites are provided by the helical domains which assemble in a criss-cross fashion to form a helical filament.	DISCUSS
20	34	assembly sites	site	In dynamin, further assembly sites are provided by the helical domains which assemble in a criss-cross fashion to form a helical filament.	DISCUSS
55	70	helical domains	structure_element	In dynamin, further assembly sites are provided by the helical domains which assemble in a criss-cross fashion to form a helical filament.	DISCUSS
121	137	helical filament	structure_element	In dynamin, further assembly sites are provided by the helical domains which assemble in a criss-cross fashion to form a helical filament.	DISCUSS
3	60	dynamin-related Eps15 homology domain containing proteins	protein_type	In dynamin-related Eps15 homology domain containing proteins (EHDs), a second assembly interface is present in the GTPase domain.	DISCUSS
62	66	EHDs	protein_type	In dynamin-related Eps15 homology domain containing proteins (EHDs), a second assembly interface is present in the GTPase domain.	DISCUSS
71	96	second assembly interface	site	In dynamin-related Eps15 homology domain containing proteins (EHDs), a second assembly interface is present in the GTPase domain.	DISCUSS
115	128	GTPase domain	structure_element	In dynamin-related Eps15 homology domain containing proteins (EHDs), a second assembly interface is present in the GTPase domain.	DISCUSS
4	9	Irga6	protein	For Irga6, additional interfaces in the helical domain are presumably involved in oligomerization, such as the secondary patch residues whose mutation prevented oligomerization in the crystallized mutant.	DISCUSS
22	32	interfaces	site	For Irga6, additional interfaces in the helical domain are presumably involved in oligomerization, such as the secondary patch residues whose mutation prevented oligomerization in the crystallized mutant.	DISCUSS
40	54	helical domain	structure_element	For Irga6, additional interfaces in the helical domain are presumably involved in oligomerization, such as the secondary patch residues whose mutation prevented oligomerization in the crystallized mutant.	DISCUSS
111	126	secondary patch	site	For Irga6, additional interfaces in the helical domain are presumably involved in oligomerization, such as the secondary patch residues whose mutation prevented oligomerization in the crystallized mutant.	DISCUSS
142	150	mutation	experimental_method	For Irga6, additional interfaces in the helical domain are presumably involved in oligomerization, such as the secondary patch residues whose mutation prevented oligomerization in the crystallized mutant.	DISCUSS
184	196	crystallized	evidence	For Irga6, additional interfaces in the helical domain are presumably involved in oligomerization, such as the secondary patch residues whose mutation prevented oligomerization in the crystallized mutant.	DISCUSS
197	203	mutant	protein_state	For Irga6, additional interfaces in the helical domain are presumably involved in oligomerization, such as the secondary patch residues whose mutation prevented oligomerization in the crystallized mutant.	DISCUSS
8	26	structural studies	experimental_method	Further structural studies, especially electron microscopy analysis of the Irga6 oligomers, are required to clarify the assembly mode via the helical domains and to show how these interfaces cooperate with the G interface to mediate the regulated assembly on a membrane surface.	DISCUSS
39	67	electron microscopy analysis	experimental_method	Further structural studies, especially electron microscopy analysis of the Irga6 oligomers, are required to clarify the assembly mode via the helical domains and to show how these interfaces cooperate with the G interface to mediate the regulated assembly on a membrane surface.	DISCUSS
75	80	Irga6	protein	Further structural studies, especially electron microscopy analysis of the Irga6 oligomers, are required to clarify the assembly mode via the helical domains and to show how these interfaces cooperate with the G interface to mediate the regulated assembly on a membrane surface.	DISCUSS
81	90	oligomers	oligomeric_state	Further structural studies, especially electron microscopy analysis of the Irga6 oligomers, are required to clarify the assembly mode via the helical domains and to show how these interfaces cooperate with the G interface to mediate the regulated assembly on a membrane surface.	DISCUSS
142	157	helical domains	structure_element	Further structural studies, especially electron microscopy analysis of the Irga6 oligomers, are required to clarify the assembly mode via the helical domains and to show how these interfaces cooperate with the G interface to mediate the regulated assembly on a membrane surface.	DISCUSS
180	190	interfaces	site	Further structural studies, especially electron microscopy analysis of the Irga6 oligomers, are required to clarify the assembly mode via the helical domains and to show how these interfaces cooperate with the G interface to mediate the regulated assembly on a membrane surface.	DISCUSS
210	221	G interface	site	Further structural studies, especially electron microscopy analysis of the Irga6 oligomers, are required to clarify the assembly mode via the helical domains and to show how these interfaces cooperate with the G interface to mediate the regulated assembly on a membrane surface.	DISCUSS
56	70	helical domain	structure_element	Notably, we did not observe major rearrangements of the helical domain versus the GTPase domain in the Irga6 molecules that dimerized via the G interface.	DISCUSS
82	95	GTPase domain	structure_element	Notably, we did not observe major rearrangements of the helical domain versus the GTPase domain in the Irga6 molecules that dimerized via the G interface.	DISCUSS
103	108	Irga6	protein	Notably, we did not observe major rearrangements of the helical domain versus the GTPase domain in the Irga6 molecules that dimerized via the G interface.	DISCUSS
124	133	dimerized	protein_state	Notably, we did not observe major rearrangements of the helical domain versus the GTPase domain in the Irga6 molecules that dimerized via the G interface.	DISCUSS
142	153	G interface	site	Notably, we did not observe major rearrangements of the helical domain versus the GTPase domain in the Irga6 molecules that dimerized via the G interface.	DISCUSS
23	27	BDLP	protein_type	In a manner similar to BDLP, such large-scale conformational changes may be induced by membrane binding.	DISCUSS
4	23	structural analysis	experimental_method	Our structural analysis and the identification of the G-interface paves the way for determining the specific assembly of Irga6 into a membrane-associated scaffold as the prerequisite to understand its action as an anti-parasitic machine.	DISCUSS
54	65	G-interface	site	Our structural analysis and the identification of the G-interface paves the way for determining the specific assembly of Irga6 into a membrane-associated scaffold as the prerequisite to understand its action as an anti-parasitic machine.	DISCUSS
121	126	Irga6	protein	Our structural analysis and the identification of the G-interface paves the way for determining the specific assembly of Irga6 into a membrane-associated scaffold as the prerequisite to understand its action as an anti-parasitic machine.	DISCUSS
25	28	Irg	protein_type	Our study indicates that Irg proteins dimerize via the G interface in a parallel head-to-head fashion thereby facilitating GTPase activation.	CONCL
38	46	dimerize	oligomeric_state	Our study indicates that Irg proteins dimerize via the G interface in a parallel head-to-head fashion thereby facilitating GTPase activation.	CONCL
55	66	G interface	site	Our study indicates that Irg proteins dimerize via the G interface in a parallel head-to-head fashion thereby facilitating GTPase activation.	CONCL
72	93	parallel head-to-head	protein_state	Our study indicates that Irg proteins dimerize via the G interface in a parallel head-to-head fashion thereby facilitating GTPase activation.	CONCL
123	129	GTPase	protein_type	Our study indicates that Irg proteins dimerize via the G interface in a parallel head-to-head fashion thereby facilitating GTPase activation.	CONCL
91	94	Irg	protein_type	These findings contribute to a molecular understanding of the anti-parasitic action of the Irg protein family and suggest that Irgs are bona-fide members of the dynamin superfamily.	CONCL
127	131	Irgs	protein_type	These findings contribute to a molecular understanding of the anti-parasitic action of the Irg protein family and suggest that Irgs are bona-fide members of the dynamin superfamily.	CONCL
161	168	dynamin	protein_type	These findings contribute to a molecular understanding of the anti-parasitic action of the Irg protein family and suggest that Irgs are bona-fide members of the dynamin superfamily.	CONCL