6vmb
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Chloroplast ATP synthase (C1, CF1FO)== | |
| + | <StructureSection load='6vmb' size='340' side='right'caption='[[6vmb]], [[Resolution|resolution]] 5.23Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6vmb]] is a 26 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VMB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VMB 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]] 5.23Å</td></tr> | ||
| + | <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></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=6vmb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vmb OCA], [https://pdbe.org/6vmb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vmb RCSB], [https://www.ebi.ac.uk/pdbsum/6vmb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vmb ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ATPA_SPIOL ATPA_SPIOL] Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In higher plants, chloroplast ATP synthase has a unique redox switch on its gamma subunit that modulates enzyme activity to limit ATP hydrolysis at night. To understand the molecular details of the redox modulation, we used single-particle cryo-EM to determine the structures of spinach chloroplast ATP synthase in both reduced and oxidized states. The disulfide linkage of the oxidized gamma subunit introduces a torsional constraint to stabilize the two beta hairpin structures. Once reduced, free cysteines alleviate this constraint, resulting in a concerted motion of the enzyme complex and a smooth transition between rotary states to facilitate the ATP synthesis. We added an uncompetitive inhibitor, tentoxin, in the reduced sample to limit the flexibility of the enzyme and obtained high-resolution details. Our cryo-EM structures provide mechanistic insight into the redox modulation of the energy regulation activity of chloroplast ATP synthase. | ||
| - | + | Structural basis of redox modulation on chloroplast ATP synthase.,Yang JH, Williams D, Kandiah E, Fromme P, Chiu PL Commun Biol. 2020 Sep 2;3(1):482. doi: 10.1038/s42003-020-01221-8. PMID:32879423<ref>PMID:32879423</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6vmb" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| - | [[Category: Fromme | + | ==See Also== |
| - | [[Category: | + | *[[ATPase 3D structures|ATPase 3D structures]] |
| - | [[Category: Williams | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Spinacia oleracea]] | ||
| + | [[Category: Chiu P-L]] | ||
| + | [[Category: Fromme P]] | ||
| + | [[Category: Kandiah E]] | ||
| + | [[Category: Williams D]] | ||
| + | [[Category: Yang J-H]] | ||
Current revision
Chloroplast ATP synthase (C1, CF1FO)
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