3u32

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3u32]] 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=3U32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U32 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3u32]] 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=3U32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U32 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCW:DICYCLOHEXYLUREA'>DCW</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='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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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCW:DICYCLOHEXYLUREA'>DCW</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></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]], [[2wgm|2wgm]], [[3u2f|3u2f]], [[3u2y|3u2y]]</div></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3u32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u32 OCA], [https://pdbe.org/3u32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u32 RCSB], [https://www.ebi.ac.uk/pdbsum/3u32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u32 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=3u32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u32 OCA], [https://pdbe.org/3u32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u32 RCSB], [https://www.ebi.ac.uk/pdbsum/3u32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u32 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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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Faraldo-Gomez, J]]
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[[Category: Faraldo-Gomez J]]
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[[Category: Krah, A]]
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[[Category: Krah A]]
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[[Category: Meier, T]]
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[[Category: Meier T]]
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[[Category: Mueller, D M]]
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[[Category: Mueller DM]]
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[[Category: Osowski, D]]
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[[Category: Osowski D]]
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[[Category: Pagadala, V]]
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[[Category: Pagadala V]]
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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: Dccd-reacted]]
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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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Current revision

ATP synthase c10 ring reacted with DCCD at pH 5.5

PDB ID 3u32

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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