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8h9u
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Human ATP synthase state 3a (combined)== | |
| - | + | <StructureSection load='8h9u' size='340' side='right'caption='[[8h9u]], [[Resolution|resolution]] 2.61Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8h9u]] is a 17 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H9U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H9U FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.61Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8h9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h9u OCA], [https://pdbe.org/8h9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h9u RCSB], [https://www.ebi.ac.uk/pdbsum/8h9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h9u ProSAT]</span></td></tr> |
| - | [[Category: Gao | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: Lai | + | [https://www.uniprot.org/uniprot/ATPG_HUMAN ATPG_HUMAN] 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(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.[UniProtKB:P05631] |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gao Y]] | ||
| + | [[Category: Gong H]] | ||
| + | [[Category: Lai Y]] | ||
| + | [[Category: Liu F]] | ||
| + | [[Category: Rao Z]] | ||
| + | [[Category: Zhang Y]] | ||
Current revision
Human ATP synthase state 3a (combined)
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Categories: Homo sapiens | Large Structures | Gao Y | Gong H | Lai Y | Liu F | Rao Z | Zhang Y
