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| ==Subcomplex of the stator of bovine mitochondrial ATP synthase== | | ==Subcomplex of the stator of bovine mitochondrial ATP synthase== |
| <StructureSection load='2cly' size='340' side='right' caption='[[2cly]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='2cly' size='340' side='right'caption='[[2cly]], [[Resolution|resolution]] 2.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[2cly]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CLY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CLY FirstGlance]. <br> | | <table><tr><td colspan='2'>[[2cly]] is a 6 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=2CLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CLY FirstGlance]. <br> |
| </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1vzs|1vzs]]</td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=2cly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cly OCA], [https://pdbe.org/2cly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cly RCSB], [https://www.ebi.ac.uk/pdbsum/2cly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cly ProSAT]</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=2cly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cly OCA], [http://pdbe.org/2cly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cly RCSB], [http://www.ebi.ac.uk/pdbsum/2cly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cly ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == Function == | | == Function == |
| [[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/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/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. | | [https://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. |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| </div> | | </div> |
| <div class="pdbe-citations 2cly" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2cly" style="background-color:#fffaf0;"></div> |
| | |
| | ==See Also== |
| | *[[ATPase 3D structures|ATPase 3D structures]] |
| == References == | | == References == |
| <references/> | | <references/> |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bovin]] | | [[Category: Bos taurus]] |
| [[Category: Dickson, V Kane]] | | [[Category: Large Structures]] |
| [[Category: Fearnley, I M]] | | [[Category: Fearnley IM]] |
| [[Category: Leslie, A G.W]] | | [[Category: Kane Dickson V]] |
| [[Category: Silvester, J A]] | | [[Category: Leslie AGW]] |
| [[Category: Walker, J E]] | | [[Category: Silvester JA]] |
| [[Category: Acetylation]] | | [[Category: Walker JE]] |
| [[Category: Atp synthase]]
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| [[Category: Hydrogen ion transport]]
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| [[Category: Hydrolase]]
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| [[Category: Ion transport]]
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| [[Category: Mitochondria]]
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| [[Category: Mitochondrion]]
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| [[Category: Peripheral stalk]]
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| [[Category: Stator]]
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| [[Category: Transit peptide]]
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| [[Category: Transport]]
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