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+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