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3u32
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3u32 is ON HOLD until Paper Publication Authors: Symersky, J., Pagadala, V., Osowski, D., Krah, A., Meier, T., Faraldo-Gomez, J., Mueller, D.M. Des...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==ATP synthase c10 ring reacted with DCCD at pH 5.5== | |
| + | <StructureSection load='3u32' size='340' side='right'caption='[[3u32]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == 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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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>, <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=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> | ||
| + | == Function == | ||
| + | [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. | ||
| - | + | ==See Also== | |
| - | + | *[[ATPase 3D structures|ATPase 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Faraldo-Gomez J]] | ||
| + | [[Category: Krah A]] | ||
| + | [[Category: Meier T]] | ||
| + | [[Category: Mueller DM]] | ||
| + | [[Category: Osowski D]] | ||
| + | [[Category: Pagadala V]] | ||
| + | [[Category: Symersky J]] | ||
Current revision
ATP synthase c10 ring reacted with DCCD at pH 5.5
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