4cbk

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<StructureSection load='4cbk' size='340' side='right'caption='[[4cbk]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
<StructureSection load='4cbk' size='340' side='right'caption='[[4cbk]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4cbk]] 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=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>
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<table><tr><td colspan='2'>[[4cbk]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Alkalihalophilus_pseudofirmus_OF4 Alkalihalophilus pseudofirmus OF4]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4CBK FirstGlance]. <br>
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</td></tr><tr id='ligand'><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></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DPV:DODECYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>DPV</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cbk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cbk OCA], [https://pdbe.org/4cbk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cbk RCSB], [https://www.ebi.ac.uk/pdbsum/4cbk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbk ProSAT]</span></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cbj|4cbj]]</td></tr>
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<tr id='resources'><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://pdbe.org/4cbk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cbk RCSB], [http://www.ebi.ac.uk/pdbsum/4cbk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cbk ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/ATPL_ALKPO ATPL_ALKPO]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4cbk" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[ATPase|ATPase]]
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*[[ATPase 3D structures|ATPase 3D structures]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus pseudofirmus of4]]
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[[Category: Alkalihalophilus pseudofirmus OF4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Meier, T]]
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[[Category: Meier T]]
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[[Category: Preiss, L]]
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[[Category: Preiss L]]
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[[Category: Yildiz, O]]
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[[Category: Yildiz O]]
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[[Category: C-ring rotor]]
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[[Category: F1fo-atp synthase]]
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[[Category: Ion binding pocket]]
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[[Category: Transferase]]
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Revision as of 17:37, 7 September 2022

The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic cell physiology

PDB ID 4cbk

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