3ud0

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[[Image:3ud0.png|left|200px]]
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==ATP synthase C10 ring in proton-unlocked conformation at PH 5.5==
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<StructureSection load='3ud0' size='340' side='right' caption='[[3ud0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ud0]] 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=3UD0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UD0 FirstGlance]. <br>
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</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>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xok|2xok]], [[2xqu|2xqu]], [[2x2v|2x2v]], [[3u2f|3u2f]], [[3u2y|3u2y]], [[3u32|3u32]]</td></tr>
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<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=3ud0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ud0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ud0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ud0 PDBsum]</span></td></tr>
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<table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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The line below this paragraph, containing "STRUCTURE_3ud0", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_3ud0| PDB=3ud0 | SCENE= }}
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===ATP synthase C10 ring in proton-unlocked conformation at PH 5.5===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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==See Also==
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*[[ATP synthase|ATP synthase]]
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The line below this paragraph, {{ABSTRACT_PUBMED_22504883}}, adds the Publication Abstract to the page
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*[[ATPase|ATPase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 22504883 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22504883}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[3ud0]] 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=3UD0 OCA].
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==Reference==
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<ref group="xtra">PMID:022504883</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Mueller, D.]]
[[Category: Mueller, D.]]

Revision as of 06:33, 5 June 2014

ATP synthase C10 ring in proton-unlocked conformation at PH 5.5

3ud0, resolution 2.00Å

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