2xqs: Difference between revisions
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== | ==Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases== | ||
[[2xqs]] is a 5 chain structure with sequence from [ | <StructureSection load='2xqs' size='340' side='right'caption='[[2xqs]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xqs]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XQS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CVM:CYMAL-4'>CVM</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</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=2xqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xqs OCA], [https://pdbe.org/2xqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xqs RCSB], [https://www.ebi.ac.uk/pdbsum/2xqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xqs ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The microscopic mechanism of coupled c-ring rotation and ion translocation in F(1)F(o)-ATP synthases is unknown. Here we present conclusive evidence supporting the notion that the ability of c-rings to rotate within the F(o) complex derives from the interplay between the ion-binding sites and their nonhomogenous microenvironment. This evidence rests on three atomic structures of the c(15) rotor from crystals grown at low pH, soaked at high pH and, after N,N'-dicyclohexylcarbodiimide (DCCD) modification, resolved at 1.8, 3.0 and 2.2 A, respectively. Alongside a quantitative DCCD-labeling assay and free-energy molecular dynamics calculations, these data demonstrate how the thermodynamic stability of the so-called proton-locked state is maximized by the lipid membrane. By contrast, a hydrophilic environment at the a-subunit-c-ring interface appears to unlock the binding-site conformation and promotes proton exchange with the surrounding solution. Rotation thus occurs as c-subunits stochastically alternate between these environments, directionally biased by the electrochemical transmembrane gradient. | |||
Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases.,Pogoryelov D, Krah A, Langer JD, Yildiz O, Faraldo-Gomez JD, Meier T Nat Chem Biol. 2010 Dec;6(12):891-9. Epub 2010 Oct 24. PMID:20972431<ref>PMID:20972431</ref> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xqs" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arthrospira platensis]] | [[Category: Arthrospira platensis]] | ||
[[Category: Faraldo-Gomez | [[Category: Large Structures]] | ||
[[Category: Krah | [[Category: Faraldo-Gomez JD]] | ||
[[Category: Langer | [[Category: Krah A]] | ||
[[Category: Meier | [[Category: Langer J]] | ||
[[Category: Pogoryelov | [[Category: Meier T]] | ||
[[Category: Yildiz | [[Category: Pogoryelov D]] | ||
[[Category: Yildiz O]] | |||
