3ud0

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ud0]] is a 5 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=3UD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UD0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ud0]] is a 5 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=3UD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UD0 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xok|2xok]], [[2xqu|2xqu]], [[2x2v|2x2v]], [[3u2f|3u2f]], [[3u2y|3u2y]], [[3u32|3u32]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3ud0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ud0 OCA], [https://pdbe.org/3ud0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ud0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ud0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ud0 ProSAT]</span></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=3ud0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ud0 OCA], [https://pdbe.org/3ud0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ud0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ud0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ud0 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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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[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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<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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3ud0" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Mueller, D]]
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[[Category: Mueller D]]
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[[Category: Symersky, J]]
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[[Category: Symersky J]]
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[[Category: C10 ring]]
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[[Category: F1fo atp synthase]]
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[[Category: Membrane protein]]
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[[Category: Proton pore]]
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Revision as of 13:55, 14 March 2024

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

PDB ID 3ud0

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