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==CryoEM structure of Polytomella F-ATP synthase, Primary rotary state 1, focussed refinement of F1 head and rotor== | |||
<StructureSection load='6rdb' size='340' side='right'caption='[[6rdb]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6rdb]] is a 20 chain structure with sequence from [http://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=6RDB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RDB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/H(+)-transporting_two-sector_ATPase H(+)-transporting two-sector ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.1.2.2 7.1.2.2] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6rdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rdb OCA], [http://pdbe.org/6rdb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rdb RCSB], [http://www.ebi.ac.uk/pdbsum/6rdb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rdb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0ZW40_9CHLO A0ZW40_9CHLO]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[RuleBase:RU003551] [[http://www.uniprot.org/uniprot/A0ZW41_9CHLO A0ZW41_9CHLO]] Produces ATP from ADP in the presence of a proton gradient across the membrane.[RuleBase:RU003553] | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6rdb" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Polytomella sp. pringsheim 198 80]] | |||
[[Category: Klusch, N]] | [[Category: Klusch, N]] | ||
[[Category: Kuhlbrandt, W]] | [[Category: Kuhlbrandt, W]] | ||
[[Category: Murphy, B | [[Category: Murphy, B J]] | ||
[[Category: Yildiz, O]] | |||
[[Category: Mitochondrial atp synthase dimer flexible coupling cryoem]] | |||
[[Category: Proton transport]] | |||
Revision as of 09:04, 3 July 2019
CryoEM structure of Polytomella F-ATP synthase, Primary rotary state 1, focussed refinement of F1 head and rotorCryoEM structure of Polytomella F-ATP synthase, Primary rotary state 1, focussed refinement of F1 head and rotor
Structural highlights
Function[A0ZW40_9CHLO] Produces ATP from ADP in the presence of a proton gradient across the membrane.[RuleBase:RU003551] [A0ZW41_9CHLO] Produces ATP from ADP in the presence of a proton gradient across the membrane.[RuleBase:RU003553] Publication Abstract from PubMedF1Fo-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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