3u2f: Difference between revisions
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[[ | ==ATP synthase c10 ring in proton-unlocked conformation at PH 8.3== | ||
<StructureSection load='3u2f' size='340' side='right' caption='[[3u2f]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3u2f]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U2F FirstGlance]. <br> | |||
</td></tr><tr><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xok|2xok]], [[2xqu|2xqu]], [[2x2v|2x2v]], [[2wgm|2wgm]], [[3u2y|3u2y]], [[3u32|3u32]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u2f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u2f RCSB], [http://www.ebi.ac.uk/pdbsum/3u2f PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The proton pore of the F(1)F(o) ATP synthase consists of a ring of c subunits, which rotates, driven by downhill proton diffusion across the membrane. An essential carboxylate side chain in each subunit provides a proton-binding site. In all the structures of c-rings reported to date, these sites are in a closed, ion-locked state. Structures are here presented of the c(10) ring from Saccharomyces cerevisiae determined at pH 8.3, 6.1 and 5.5, at resolutions of 2.0 A, 2.5 A and 2.0 A, respectively. The overall structure of this mitochondrial c-ring is similar to known homologs, except that the essential carboxylate, Glu59, adopts an open extended conformation. Molecular dynamics simulations reveal that opening of the essential carboxylate is a consequence of the amphiphilic nature of the crystallization buffer. We propose that this new structure represents the functionally open form of the c subunit, which facilitates proton loading and release. | |||
Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.,Symersky J, Pagadala V, Osowski D, Krah A, Meier T, Faraldo-Gomez JD, Mueller DM Nat Struct Mol Biol. 2012 Apr 15;19(5):485-91. doi: 10.1038/nsmb.2284. PMID:22504883<ref>PMID:22504883</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[ATP synthase|ATP synthase]] | |||
*[[ATPase|ATPase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Faraldo-Gomez, J.]] | [[Category: Faraldo-Gomez, J.]] | ||
Revision as of 06:35, 5 June 2014
ATP synthase c10 ring in proton-unlocked conformation at PH 8.3
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