6voi: Difference between revisions

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-'''Unreleased structure'''
-The entry 6voi is ON HOLD
+==Chloroplast ATP synthase (O1, CF1)==
+<StructureSection load='6voi' size='340' side='right'caption='[[6voi]], [[Resolution|resolution]] 4.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6voi]] is a 9 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=6VOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VOI 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]] 4.03&#8491;</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=6voi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6voi OCA], [https://pdbe.org/6voi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6voi RCSB], [https://www.ebi.ac.uk/pdbsum/6voi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6voi ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATPG_SPIOL ATPG_SPIOL] Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
+<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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6voi" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ATPase 3D structures|ATPase 3D structures]]
+== 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]]