View source for 9vpc


==Cryo-EM structure of the IF1 bound bovine ATP synthase tetramer==
<StructureSection load='9vpc' size='340' side='right'caption='[[9vpc]], [[Resolution|resolution]] 7.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vpc]] is a 68 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=9VPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VPC 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]] 7.2&#8491;</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=9vpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vpc OCA], [https://pdbe.org/9vpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vpc RCSB], [https://www.ebi.ac.uk/pdbsum/9vpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vpc ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Gerle C]]
[[Category: Jiko C]]
[[Category: Nakano A]]
[[Category: Yamashita E]]
[[Category: Yokoyama K]]