4cbj: Difference between revisions

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'''Unreleased structure'''
==The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology==
<StructureSection load='4cbj' size='340' side='right' caption='[[4cbj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4cbj]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_pseudofirmus_of4 Bacillus pseudofirmus of4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CBJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CBJ 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=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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">[[4cbk|4cbk]]</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=4cbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cbj RCSB], [http://www.ebi.ac.uk/pdbsum/4cbj 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 entry 4cbj is ON HOLD  until sometime in the future
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>


Authors: Preiss, L., Yildiz, O., Meier, T.
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus pseudofirmus of4]]
[[Category: Meier, T.]]
[[Category: Preiss, L.]]
[[Category: Yildiz, O.]]
[[Category: C-ring rotor]]
[[Category: F1fo-atp synthase]]
[[Category: Ion binding pocket]]
[[Category: Transferase]]
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