View source for 6red


==Cryo-EM structure of Polytomella F-ATP synthase, Rotary substate 3A, focussed refinement of F1 head and rotor==
<SX load='6red' size='340' side='right' viewer='molstar' caption='[[6red]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6red]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Polytomella_sp._Pringsheim_198.80 Polytomella sp. Pringsheim 198.80]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RED 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]] 3&#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=6red FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6red OCA], [https://pdbe.org/6red PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6red RCSB], [https://www.ebi.ac.uk/pdbsum/6red PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6red ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D7P7X5_9CHLO D7P7X5_9CHLO] 
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== Publication Abstract from PubMed ==
F1Fo-adenosine triphosphate (ATP) synthases make the energy of the proton-motive force available for energy-consuming processes in the cell. We determined the single-particle cryo-electron microscopy structure of active dimeric ATP synthase from mitochondria of Polytomella sp. at a resolution of 2.7 to 2.8 angstroms. Separation of 13 well-defined rotary substates by three-dimensional classification provides a detailed picture of the molecular motions that accompany c-ring rotation and result in ATP synthesis. Crucially, the F1 head rotates along with the central stalk and c-ring rotor for the first ~30 degrees of each 120 degrees primary rotary step to facilitate flexible coupling of the stoichiometrically mismatched F1 and Fo subcomplexes. Flexibility is mediated primarily by the interdomain hinge of the conserved OSCP subunit. A conserved metal ion in the proton access channel may synchronize c-ring protonation with rotation.

Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F1-Fo coupling.,Murphy BJ, Klusch N, Langer J, Mills DJ, Yildiz O, Kuhlbrandt W Science. 2019 Jun 21;364(6446). pii: 364/6446/eaaw9128. doi:, 10.1126/science.aaw9128. Epub 2019 Jun 20. PMID:31221832<ref>PMID:31221832</ref>

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

==See Also==
*[[ATPase 3D structures|ATPase 3D structures]]
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Polytomella sp. Pringsheim 198 80]]
[[Category: Klusch N]]
[[Category: Kuhlbrandt W]]
[[Category: Murphy BJ]]
[[Category: Yildiz O]]