7tk3: Difference between revisions
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==Yeast ATP synthase State 1binding(b) with 10 mM ATP backbone model== | ==Yeast ATP synthase State 1binding(b) with 10 mM ATP backbone model== | ||
<StructureSection load='7tk3' size='340' side='right'caption='[[7tk3]]' scene=''> | <StructureSection load='7tk3' size='340' side='right'caption='[[7tk3]], [[Resolution|resolution]] 6.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TK3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7tk3]] is a 23 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TK3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TK3 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=7tk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tk3 OCA], [https://pdbe.org/7tk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tk3 RCSB], [https://www.ebi.ac.uk/pdbsum/7tk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tk3 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]] 6.3Å</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=7tk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tk3 OCA], [https://pdbe.org/7tk3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tk3 RCSB], [https://www.ebi.ac.uk/pdbsum/7tk3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tk3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ATP9_YEAST ATP9_YEAST] 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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Guo H]] | [[Category: Guo H]] | ||
[[Category: Rubinstein JL]] | [[Category: Rubinstein JL]] | ||
Latest revision as of 13:54, 21 February 2024
Yeast ATP synthase State 1binding(b) with 10 mM ATP backbone modelYeast ATP synthase State 1binding(b) with 10 mM ATP backbone model
Structural highlights
FunctionATP9_YEAST 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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. See Also |
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