4cbk
From Proteopedia
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| - | + | ==The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology== | |
| - | + | <StructureSection load='4cbk' size='340' side='right' caption='[[4cbk]], [[Resolution|resolution]] 2.42Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4cbk]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacpe Bacpe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBK FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><br> | ||
| + | <tr><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cbj|4cbj]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbk RCSB], [http://www.ebi.ac.uk/pdbsum/4cbk PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In the c-ring rotor of ATP synthases ions are shuttled across the membrane during ATP synthesis by a unique rotary mechanism. We investigated characteristics of the c-ring from the alkaliphile Bacillus pseudofirmus OF4 with respect to evolutionary adaptations to operate with protons at high environmental pH. The X-ray structures of the wild-type c13 ring at pH 9.0 and a 'neutralophile-like' mutant (P51A) at pH 4.4, at 2.4 and 2.8 A resolution, respectively, reveal a dependency of the conformation and protonation state of the proton-binding glutamate (E54 ) on environmental hydrophobicity. Faster labeling kinetics with the inhibitor dicyclohexylcarbodiimide (DCCD) demonstrate a greater flexibility of E54 in the mutant due to reduced water occupancy within the H+ -binding site. A second 'neutralophile-like' mutant (V21N) shows reduced growth at high pH, which is explained by restricted conformational freedom of the mutant's E54 carboxylate. The study directly connects subtle structural adaptations of the c-ring ion-binding site to in vivo effects of alkaliphile cell physiology. | ||
| - | + | The c-ring ion-binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.,Preiss L, Langer JD, Hicks DB, Liu J, Yildiz O, Krulwich TA, Meier T Mol Microbiol. 2014 Apr 8. doi: 10.1111/mmi.12605. PMID:24707994<ref>PMID:24707994</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacpe]] | ||
[[Category: Meier, T.]] | [[Category: Meier, T.]] | ||
[[Category: Preiss, L.]] | [[Category: Preiss, L.]] | ||
Revision as of 06:40, 11 June 2014
The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology
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