5are - Revision history

OCA at 11:43, 9 May 2024

OCA — Thu, 09 May 2024 11:43:19 GMT

←Older revision		Revision as of 11:43, 9 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5are]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ARE FirstGlance]. <br>		<table><tr><td colspan='2'>[[5are]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ARE FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [https://pdbe.org/5are PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [https://www.ebi.ac.uk/pdbsum/5are PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5are ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 7.4Å</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [https://pdbe.org/5are PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [https://www.ebi.ac.uk/pdbsum/5are PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5are ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 06:25, 31 May 2023

OCA — Wed, 31 May 2023 06:25:42 GMT

←Older revision		Revision as of 06:25, 31 May 2023
Line 3:		Line 3:
	<SX load='5are' size='340' side='right' viewer='molstar' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>		<SX load='5are' size='340' side='right' viewer='molstar' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5are]] is a 22 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bos_taurus Bos taurus~~] and [http://en.wikipedia.org/wiki/Bovin Bovin~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5ARE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5are]] is a 21 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ARE FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5arh\|5arh]], [[5ari\|5ari]], [[5fij\|5fij]], [[5fik\|5fik]], [[5fil\|5fil]]</td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [https://pdbe.org/5are PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [https://www.ebi.ac.uk/pdbsum/5are PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5are ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [~~http~~://pdbe.org/5are PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5are PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5are ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/ATP6_BOVIN ATP6_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. [[http://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/ATPO_BOVIN ATPO_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. [[http://www.uniprot.org/uniprot/ATP5H_BOVIN ATP5H_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. [[http://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/AT5F1_BOVIN AT5F1_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. [[http://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[http://www.uniprot.org/uniprot/ATPD_BOVIN ATPD_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/ATP5J_BOVIN ATP5J_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes. [[http://www.uniprot.org/uniprot/ATP5E_BOVIN ATP5E_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.	+	[https://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 25:
	</SX>		</SX>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Bovin]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bason~~, J V~~]]	+	[[Category: Bason JV]]
-	[[Category: Grigorieff, N]]	+	[[Category: Grigorieff N]]
-	[[Category: Montgomery~~, M G~~]]	+	[[Category: Montgomery MG]]
-	[[Category: Rohou, A]]	+	[[Category: Rohou A]]
-	[[Category: Rubinstein~~, J L~~]]	+	[[Category: Rubinstein JL]]
-	[[Category: Schep~~, D G~~]]	+	[[Category: Schep DG]]
-	[[Category: Walker~~, J E~~]]	+	[[Category: Walker JE]]
-	[[Category: Zhou, A]]	+	[[Category: Zhou A]]
-	~~[[Category: Atp synthase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Rotary atpase~~]]	+

OCA at 19:47, 10 April 2020

OCA — Fri, 10 Apr 2020 19:47:31 GMT

←Older revision		Revision as of 19:47, 10 April 2020
Line 3:		Line 3:
	<SX load='5are' size='340' side='right' viewer='molstar' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>		<SX load='5are' size='340' side='right' viewer='molstar' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5are]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5ARE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5are]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ARE FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5arh\|5arh]], [[5ari\|5ari]], [[5fij\|5fij]], [[5fik\|5fik]], [[5fil\|5fil]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5arh\|5arh]], [[5ari\|5ari]], [[5fij\|5fij]], [[5fik\|5fik]], [[5fil\|5fil]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [http://pdbe.org/5are PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [http://www.ebi.ac.uk/pdbsum/5are PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5are ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [http://pdbe.org/5are PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [http://www.ebi.ac.uk/pdbsum/5are PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5are ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 18:12, 6 March 2020

OCA — Fri, 06 Mar 2020 18:12:37 GMT

←Older revision		Revision as of 18:12, 6 March 2020
Line 1:		Line 1:

	==Bovine mitochondrial ATP synthase state 1b==		==Bovine mitochondrial ATP synthase state 1b==
-	<~~StructureSection~~ load='5are' size='340' side='right' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>	+	<SX load='5are' size='340' side='right' viewer='molstar' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5are]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ARE FirstGlance]. <br>		<table><tr><td colspan='2'>[[5are]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ARE FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5are" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5are" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ATPase 3D structures\|ATPase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
-	</~~StructureSection~~>	+	</SX>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Bovin]]		[[Category: Bovin]]
		+	[[Category: Large Structures]]
	[[Category: Bason, J V]]		[[Category: Bason, J V]]
	[[Category: Grigorieff, N]]		[[Category: Grigorieff, N]]

OCA at 03:10, 16 November 2017

OCA — Thu, 16 Nov 2017 03:10:20 GMT

←Older revision		Revision as of 03:10, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='5are' size='340' side='right' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>		<StructureSection load='5are' size='340' side='right' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5are]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/~~Bos_taurus Bos taurus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ARE FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5are]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ARE FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5arh\|5arh]], [[5ari\|5ari]], [[5fij\|5fij]], [[5fik\|5fik]], [[5fil\|5fil]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5arh\|5arh]], [[5ari\|5ari]], [[5fij\|5fij]], [[5fik\|5fik]], [[5fil\|5fil]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5are" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5are" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[ATPase\|ATPase]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
		+	[[Category: Bovin]]
	[[Category: Bason, J V]]		[[Category: Bason, J V]]
	[[Category: Grigorieff, N]]		[[Category: Grigorieff, N]]

OCA at 06:03, 19 April 2017

OCA — Wed, 19 Apr 2017 06:03:35 GMT

←Older revision		Revision as of 06:03, 19 April 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5are" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5are" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[ATPase\|ATPase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:11, 22 December 2016

OCA — Thu, 22 Dec 2016 14:11:36 GMT

←Older revision		Revision as of 14:11, 22 December 2016
Line 6:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5arh\|5arh]], [[5ari\|5ari]], [[5fij\|5fij]], [[5fik\|5fik]], [[5fil\|5fil]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5arh\|5arh]], [[5ari\|5ari]], [[5fij\|5fij]], [[5fik\|5fik]], [[5fil\|5fil]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [http://pdbe.org/5are PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [http://www.ebi.ac.uk/pdbsum/5are PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [http://pdbe.org/5are PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [http://www.ebi.ac.uk/pdbsum/5are PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5are ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 04:31, 11 May 2016

OCA — Wed, 11 May 2016 04:31:27 GMT

←Older revision		Revision as of 04:31, 11 May 2016
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		+
	==Bovine mitochondrial ATP synthase state 1b==		==Bovine mitochondrial ATP synthase state 1b==
	<StructureSection load='5are' size='340' side='right' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>		<StructureSection load='5are' size='340' side='right' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>

OCA at 03:49, 16 October 2015

OCA — Fri, 16 Oct 2015 03:49:24 GMT

←Older revision		Revision as of 03:49, 16 October 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Bovine mitochondrial ATP synthase state 1b==
		+	<StructureSection load='5are' size='340' side='right' caption='[[5are]], [[Resolution\|resolution]] 7.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5are]] is a 22 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ARE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ARE FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5arh\|5arh]], [[5ari\|5ari]], [[5fij\|5fij]], [[5fik\|5fik]], [[5fil\|5fil]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.14 3.6.3.14] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5are OCA], [http://pdbe.org/5are PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5are RCSB], [http://www.ebi.ac.uk/pdbsum/5are PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ATP6_BOVIN ATP6_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane. [[http://www.uniprot.org/uniprot/ATPG_BOVIN ATPG_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/ATPO_BOVIN ATPO_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. [[http://www.uniprot.org/uniprot/ATP5H_BOVIN ATP5H_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. [[http://www.uniprot.org/uniprot/ATPB_BOVIN ATPB_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/AT5F1_BOVIN AT5F1_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. [[http://www.uniprot.org/uniprot/ATPA_BOVIN ATPA_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). [[http://www.uniprot.org/uniprot/ATPD_BOVIN ATPD_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP turnover in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. [[http://www.uniprot.org/uniprot/ATP5J_BOVIN ATP5J_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes. [[http://www.uniprot.org/uniprot/ATP5E_BOVIN ATP5E_BOVIN]] Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Adenosine triphosphate (ATP), the chemical energy currency of biology, is synthesized in eukaryotic cells primarily by the mitochondrial ATP synthase. ATP synthases operate by a rotary catalytic mechanism where proton translocation through the membrane-inserted F0 region is coupled to ATP synthesis in the catalytic F1 region via rotation of a central rotor subcomplex. We report here single particle electron cryomicroscopy (cryo-EM) analysis of the bovine mitochondrial ATP synthase. Combining cryo-EM data with bioinformatic analysis allowed us to determine the fold of the a subunit, suggesting a proton translocation path through the F0 region that involves both the a and b subunits. 3D classification of images revealed seven distinct states of the enzyme that show different modes of bending and twisting in the intact ATP synthase. Rotational fluctuations of the c8-ring within the F0 region support a Brownian ratchet mechanism for proton-translocation driven rotation in ATP synthases.

-	~~The entry 5are is ON HOLD~~	+	Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM.,Zhou A, Rohou A, Schep DG, Bason JV, Montgomery MG, Walker JE, Grigorieff N, Rubinstein JL Elife. 2015 Oct 6;4. doi: 10.7554/eLife.10180. PMID:26439008<ref>PMID:26439008</ref>

-	~~Authors: Zhou~~, A.~~, Rohou, A., Schep, D.G., Bason, J.V., Montgomery, M.G., Walker, J.E., Grigorieff, N., Rubinstein, J~~.L.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Bovine mitochondrial ATP synthase state 1b~~	+	<div class="pdbe-citations 5are" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Unreleased Structures~~]]	+	== References ==
-	[[Category: ~~Montgomery~~, ~~M.G~~]]	+	<references/>
-	[[Category: ~~Schep~~, ~~D.G~~]]	+	__TOC__
-	[[Category: ~~Rubinstein~~, ~~J.L~~]]	+	</StructureSection>
		+	[[Category: Bos taurus]]
		+	[[Category: Bason, J V]]
		+	[[Category: Grigorieff, N]]
		+	[[Category: Montgomery, M G]]
	[[Category: Rohou, A]]		[[Category: Rohou, A]]
		+	[[Category: Rubinstein, J L]]
		+	[[Category: Schep, D G]]
		+	[[Category: Walker, J E]]
	[[Category: Zhou, A]]		[[Category: Zhou, A]]
-	[[Category: ~~Grigorieff, N~~]]	+	[[Category: Atp synthase]]
-	[[Category: ~~Walker, J.E~~]]	+	[[Category: Hydrolase]]
-	[[Category: ~~Bason, J.V~~]]	+	[[Category: Rotary atpase]]

OCA at 10:44, 7 October 2015

OCA — Wed, 07 Oct 2015 10:44:50 GMT

←Older revision		Revision as of 10:44, 7 October 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5are is ON HOLD ~~until sometime in the future~~	+	The entry 5are is ON HOLD

	Authors: Zhou, A., Rohou, A., Schep, D.G., Bason, J.V., Montgomery, M.G., Walker, J.E., Grigorieff, N., Rubinstein, J.L.		Authors: Zhou, A., Rohou, A., Schep, D.G., Bason, J.V., Montgomery, M.G., Walker, J.E., Grigorieff, N., Rubinstein, J.L.