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==Structure of the yeast F1Fo ATPase c10 ring with bound oligomycin==
==Structure of the yeast F1Fo ATPase c10 ring with bound oligomycin==
<StructureSection load='4f4s' size='340' side='right' caption='[[4f4s]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4f4s' size='340' side='right'caption='[[4f4s]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4f4s]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F4S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F4S FirstGlance]. <br>
<table><tr><td colspan='2'>[[4f4s]] is a 10 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=4F4S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F4S FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EFO:OLIGOMYCIN+A'>EFO</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EFO:OLIGOMYCIN+A'>EFO</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></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=4f4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f4s OCA], [https://pdbe.org/4f4s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f4s RCSB], [https://www.ebi.ac.uk/pdbsum/4f4s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f4s ProSAT]</span></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3u2f|3u2f]], [[3u2y|3u2y]], [[3ud0|3ud0]], [[3u32|3u32]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">OLI1, ATP9, OLI3, PHO2, Q0130 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=4f4s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f4s OCA], [http://pdbe.org/4f4s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f4s RCSB], [http://www.ebi.ac.uk/pdbsum/4f4s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f4s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[ATPase|ATPase]]
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Mueller, D M]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Symersky, J]]
[[Category: Mueller DM]]
[[Category: C10 ring]]
[[Category: Symersky J]]
[[Category: F1fo atp synthase]]
[[Category: Membrane protein-antibiotic complex]]
[[Category: Mitochondria]]
[[Category: Oligomycin]]
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