5fij - Revision history

OCA at 06:52, 19 July 2023

OCA — Wed, 19 Jul 2023 06:52:32 GMT

←Older revision		Revision as of 06:52, 19 July 2023
Line 3:		Line 3:
	<SX load='5fij' size='340' side='right' viewer='molstar' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>		<SX load='5fij' size='340' side='right' viewer='molstar' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~[[5ara\|5ara]]~~, [[~~5are~~\|~~5are~~]]~~, [[5arh\|5arh]], [[5ari\|5ari]], [[5fik\|5fik]], [[5fil\|5fil]]</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='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'>[https://proteopedia.org/fgij/fg.htm?mol=5fij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fij OCA], [https://pdbe.org/5fij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fij RCSB], [https://www.ebi.ac.uk/pdbsum/5fij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fij 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=5fij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fij OCA], [~~http~~://pdbe.org/5fij PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5fij RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5fij PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5fij 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 26:
	</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 19:48, 10 April 2020

OCA — Fri, 10 Apr 2020 19:48:14 GMT

←Older revision		Revision as of 19:48, 10 April 2020
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	<SX load='5fij' size='340' side='right' viewer='molstar' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>		<SX load='5fij' size='340' side='right' viewer='molstar' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5are\|5are]], [[5arh\|5arh]], [[5ari\|5ari]], [[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]], [[5are\|5are]], [[5arh\|5arh]], [[5ari\|5ari]], [[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=5fij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fij OCA], [http://pdbe.org/5fij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fij RCSB], [http://www.ebi.ac.uk/pdbsum/5fij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fij 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=5fij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fij OCA], [http://pdbe.org/5fij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fij RCSB], [http://www.ebi.ac.uk/pdbsum/5fij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fij ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 18:12, 6 March 2020

OCA — Fri, 06 Mar 2020 18:12:52 GMT

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

	==Bovine mitochondrial ATP synthase state 2c==		==Bovine mitochondrial ATP synthase state 2c==
-	<~~StructureSection~~ load='5fij' size='340' side='right' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>	+	<SX load='5fij' size='340' side='right' viewer='molstar' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>		<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5fij" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5fij" 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 03:13, 16 November 2017

OCA — Thu, 16 Nov 2017 03:13:25 GMT

←Older revision		Revision as of 03:13, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='5fij' size='340' side='right' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>		<StructureSection load='5fij' size='340' side='right' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5are\|5are]], [[5arh\|5arh]], [[5ari\|5ari]], [[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]], [[5are\|5are]], [[5arh\|5arh]], [[5ari\|5ari]], [[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 24:		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 14:16, 22 December 2016

OCA — Thu, 22 Dec 2016 14:16:29 GMT

←Older revision		Revision as of 14:16, 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]], [[5are\|5are]], [[5arh\|5arh]], [[5ari\|5ari]], [[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]], [[5are\|5are]], [[5arh\|5arh]], [[5ari\|5ari]], [[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=5fij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fij OCA], [http://pdbe.org/5fij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fij RCSB], [http://www.ebi.ac.uk/pdbsum/5fij 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=5fij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fij OCA], [http://pdbe.org/5fij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fij RCSB], [http://www.ebi.ac.uk/pdbsum/5fij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fij ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 04:35, 11 May 2016

OCA — Wed, 11 May 2016 04:35:41 GMT

←Older revision		Revision as of 04:35, 11 May 2016
Line 1:		Line 1:
		+
	==Bovine mitochondrial ATP synthase state 2c==		==Bovine mitochondrial ATP synthase state 2c==
	<StructureSection load='5fij' size='340' side='right' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>		<StructureSection load='5fij' size='340' side='right' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>

OCA at 03:50, 16 October 2015

OCA — Fri, 16 Oct 2015 03:50:40 GMT

←Older revision		Revision as of 03:50, 16 October 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Bovine mitochondrial ATP synthase state 2c==
		+	<StructureSection load='5fij' size='340' side='right' caption='[[5fij]], [[Resolution\|resolution]] 7.40Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5fij]] 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=5FIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FIJ FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[5ara\|5ara]], [[5are\|5are]], [[5arh\|5arh]], [[5ari\|5ari]], [[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=5fij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fij OCA], [http://pdbe.org/5fij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fij RCSB], [http://www.ebi.ac.uk/pdbsum/5fij 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 5fij 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 2c~~	+	<div class="pdbe-citations 5fij" 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: Protected "5fij" [edit=sysop:move=sysop]

OCA — Wed, 07 Oct 2015 12:55:40 GMT

Protected "5fij" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:55, 7 October 2015

OCA: New page: '''Unreleased structure''' The entry 5fij 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. Descriptio...

OCA — Wed, 07 Oct 2015 12:55:38 GMT

New page: '''Unreleased structure''' The entry 5fij 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. Descriptio...

New page

'''Unreleased structure'''

The entry 5fij 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.

Description: Bovine mitochondrial ATP synthase state 2c
[[Category: Unreleased Structures]]
[[Category: Montgomery, M.G]]
[[Category: Schep, D.G]]
[[Category: Rubinstein, J.L]]
[[Category: Rohou, A]]
[[Category: Zhou, A]]
[[Category: Grigorieff, N]]
[[Category: Walker, J.E]]
[[Category: Bason, J.V]]