2xqu: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2xqu]] 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=2XQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XQU FirstGlance]. <br> | <table><tr><td colspan='2'>[[2xqu]] 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=2XQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XQU FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84Å</td></tr> | ||
<tr id=' | <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=2xqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xqu OCA], [https://pdbe.org/2xqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xqu RCSB], [https://www.ebi.ac.uk/pdbsum/2xqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xqu ProSAT]</span></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=2xqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xqu OCA], [https://pdbe.org/2xqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xqu RCSB], [https://www.ebi.ac.uk/pdbsum/2xqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xqu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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[[Category: Arthrospira platensis]] | [[Category: Arthrospira platensis]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Faraldo-Gomez | [[Category: Faraldo-Gomez JD]] | ||
[[Category: Krah | [[Category: Krah A]] | ||
[[Category: Langer | [[Category: Langer J]] | ||
[[Category: Meier | [[Category: Meier T]] | ||
[[Category: Pogoryelov | [[Category: Pogoryelov D]] | ||
[[Category: Yildiz | [[Category: Yildiz O]] | ||
Latest revision as of 13:37, 20 December 2023
Microscopic rotary mechanism of ion translocation in the Fo complex of ATP synthasesMicroscopic rotary mechanism of ion translocation in the Fo complex of ATP synthases
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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