View source for 6fkh


==Chloroplast F1Fo conformation 2==
<SX load='6fkh' size='340' side='right' viewer='molstar' caption='[[6fkh]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6fkh]] 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=6FKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FKH 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]] 4.2&#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>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=6fkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fkh OCA], [https://pdbe.org/6fkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fkh RCSB], [https://www.ebi.ac.uk/pdbsum/6fkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fkh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ATPE_SPIOL ATPE_SPIOL] Produces ATP from ADP in the presence of a proton gradient across the membrane.[HAMAP-Rule:MF_00530]
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== Publication Abstract from PubMed ==
The chloroplast adenosine triphosphate (ATP) synthase uses the electrochemical proton gradient generated by photosynthesis to produce ATP, the energy currency of all cells. Protons conducted through the membrane-embedded Fo motor drive ATP synthesis in the F1 head by rotary catalysis. We determined the high-resolution structure of the complete cF1Fo complex by cryo-electron microscopy, resolving side chains of all 26 protein subunits, the five nucleotides in the F1 head, and the proton pathway to and from the rotor ring. The flexible peripheral stalk redistributes differences in torsional energy across three unequal steps in the rotation cycle. Plant ATP synthase is autoinhibited by a beta-hairpin redox switch in subunit gamma that blocks rotation in the dark.

Structure, mechanism, and regulation of the chloroplast ATP synthase.,Hahn A, Vonck J, Mills DJ, Meier T, Kuhlbrandt W Science. 2018 May 11;360(6389). pii: 360/6389/eaat4318. doi:, 10.1126/science.aat4318. PMID:29748256<ref>PMID:29748256</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6fkh" style="background-color:#fffaf0;"></div>

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
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</SX>
[[Category: Large Structures]]
[[Category: Spinacia oleracea]]
[[Category: Hahn A]]
[[Category: Kuehlbrandt W]]
[[Category: Meier T]]
[[Category: Mills DJ]]
[[Category: Vonck J]]