8ki3
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the human ATP synthase bound to bedaquiline (composite)== | |
| - | + | <StructureSection load='8ki3' size='340' side='right'caption='[[8ki3]], [[Resolution|resolution]] 2.89Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8ki3]] is a 21 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=8KI3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8KI3 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]] 2.89Å</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=BQ1:BEDAQUILINE'>BQ1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | [[Category: Gong | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8ki3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ki3 OCA], [https://pdbe.org/8ki3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ki3 RCSB], [https://www.ebi.ac.uk/pdbsum/8ki3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ki3 ProSAT]</span></td></tr> |
| - | [[Category: Lai | + | </table> |
| - | [[Category: Zhang | + | == Disease == |
| + | [https://www.uniprot.org/uniprot/ATPA_HUMAN ATPA_HUMAN] Isolated ATP synthase deficiency. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATPA_HUMAN ATPA_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. Subunits alpha and beta form the catalytic core in F(1). 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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity). Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions (PubMed:30146159).[UniProtKB:P19483]<ref>PMID:30146159</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Gong H]] | ||
| + | [[Category: Lai Y]] | ||
| + | [[Category: Zhang Y]] | ||
Revision as of 06:20, 1 May 2024
Structure of the human ATP synthase bound to bedaquiline (composite)
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Categories: Homo sapiens | Large Structures | Gong H | Lai Y | Zhang Y
