View source for 6vog


==Chloroplast ATP synthase (O2, CF1)==
<StructureSection load='6vog' size='340' side='right'caption='[[6vog]], [[Resolution|resolution]] 4.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6vog]] 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=6VOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VOG 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]] 4.35&#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=6vog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vog OCA], [https://pdbe.org/6vog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vog RCSB], [https://www.ebi.ac.uk/pdbsum/6vog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vog 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6vog" 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]]