View source for 6cp5


==Monomer yeast ATP synthase Fo reconstituted in nanodisc with inhibitor of oligomycin bound generated from focused refinement.==
<SX load='6cp5' size='340' side='right' viewer='molstar' caption='[[6cp5]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6cp5]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CP5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6cp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cp5 OCA], [https://pdbe.org/6cp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cp5 RCSB], [https://www.ebi.ac.uk/pdbsum/6cp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cp5 ProSAT]</span></td></tr>
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== 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.
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== Publication Abstract from PubMed ==
Mitochondrial ATP synthase comprises a membrane embedded Fo motor that rotates to drive ATP synthesis in the F1 subunit. We used single-particle cryo-EM to obtain structures of the full complex in a lipid bilayer in the absence or presence of the inhibitor oligomycin, at 3.6 A and 3.8 A resolution, respectively. To limit conformational heterogeneity, we locked the rotor in a single conformation by fusing the F6 subunit of the stator with the delta-subunit of the rotor. Assembly of the enzyme with the F6-delta fusion caused a twisting of the rotor and a 9 degrees rotation of the Fo c10-ring in the direction of ATP synthesis, relative to the structure of isolated Fo Our cryo-EM structures show how F1 and Fo are coupled, give insight into the proton translocation pathway and show how oligomycin blocks ATP synthesis.

High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane.,Srivastava AP, Luo M, Zhou W, Symersky J, Bai D, Chambers MG, Faraldo-Gomez JD, Liao M, Mueller DM Science. 2018 Apr 12. pii: science.aas9699. doi: 10.1126/science.aas9699. PMID:29650704<ref>PMID:29650704</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6cp5" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Liao MF]]
[[Category: Luo M]]
[[Category: Mueller DM]]
[[Category: Srivastava AP]]
[[Category: Symersky J]]