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| | <StructureSection load='2xqt' size='340' side='right'caption='[[2xqt]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2xqt' size='340' side='right'caption='[[2xqt]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xqt]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XQT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XQT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xqt]] 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=2XQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XQT FirstGlance]. <br> |
| - | </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=DCW:DICYCLOHEXYLUREA'>DCW</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></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=DCW:DICYCLOHEXYLUREA'>DCW</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xqu|2xqu]], [[2xqs|2xqs]]</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=2xqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xqt OCA], [https://pdbe.org/2xqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xqt RCSB], [https://www.ebi.ac.uk/pdbsum/2xqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xqt ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2xqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xqt OCA], [http://pdbe.org/2xqt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xqt RCSB], [http://www.ebi.ac.uk/pdbsum/2xqt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xqt ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | [[Category: Arthrospira platensis]] | | [[Category: Arthrospira platensis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Faraldo-Gomez, J D]] | + | [[Category: Faraldo-Gomez JD]] |
| - | [[Category: Krah, A]] | + | [[Category: Krah A]] |
| - | [[Category: Langer, J]] | + | [[Category: Langer J]] |
| - | [[Category: Meier, T]] | + | [[Category: Meier T]] |
| - | [[Category: Pogoryelov, D]] | + | [[Category: Pogoryelov D]] |
| - | [[Category: Yildiz, O]] | + | [[Category: Yildiz O]] |
| - | [[Category: C-ring]]
| + | |
| - | [[Category: F1fo-atp synthase rotor]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: N\]]
| + | |
| Structural highlights
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pogoryelov D, Krah A, Langer JD, Yildiz O, Faraldo-Gomez JD, Meier T. Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases. Nat Chem Biol. 2010 Dec;6(12):891-9. Epub 2010 Oct 24. PMID:20972431 doi:10.1038/nchembio.457
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