2bs2

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[[Image:2bs2.png|left|200px]]
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==QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES==
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<StructureSection load='2bs2' size='340' side='right' caption='[[2bs2]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bs2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1qla 1qla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BS2 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e7p|1e7p]], [[1qlb|1qlb]], [[2bs3|2bs3]], [[2bs4|2bs4]]</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </span></td></tr>
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<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=2bs2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bs2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bs2 RCSB], [http://www.ebi.ac.uk/pdbsum/2bs2 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/2bs2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Membrane protein complexes can support both the generation and utilisation of a transmembrane electrochemical proton potential ('proton-motive force'), either by transmembrane electron transfer coupled to protolytic reactions on opposite sides of the membrane or by transmembrane proton transfer. Here we provide the first evidence that both of these mechanisms are combined in the case of a specific respiratory membrane protein complex, the dihaem-containing quinol:fumarate reductase (QFR) of Wolinella succinogenes, so as to facilitate transmembrane electron transfer by transmembrane proton transfer. We also demonstrate the non-functionality of this novel transmembrane proton transfer pathway ('E-pathway') in a variant QFR where a key glutamate residue has been replaced. The 'E-pathway', discussed on the basis of the 1.78-Angstrom-resolution crystal structure of QFR, can be concluded to be essential also for the viability of pathogenic varepsilon-proteobacteria such as Helicobacter pylori and is possibly relevant to proton transfer in other dihaem-containing membrane proteins, performing very different physiological functions.
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{{STRUCTURE_2bs2| PDB=2bs2 | SCENE= }}
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Evidence for transmembrane proton transfer in a dihaem-containing membrane protein complex.,Madej MG, Nasiri HR, Hilgendorff NS, Schwalbe H, Lancaster CR EMBO J. 2006 Oct 18;25(20):4963-70. Epub 2006 Oct 5. PMID:17024183<ref>PMID:17024183</ref>
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===QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_17024183}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2bs2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1qla 1qla]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BS2 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:017024183</ref><ref group="xtra">PMID:012409197</ref><ref group="xtra">PMID:011248702</ref><ref group="xtra">PMID:011186225</ref><ref group="xtra">PMID:010586875</ref><references group="xtra"/>
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[[Category: Succinate dehydrogenase]]
[[Category: Succinate dehydrogenase]]
[[Category: Wolinella succinogenes]]
[[Category: Wolinella succinogenes]]

Revision as of 09:43, 21 May 2014

See User added comments

QUINOL:FUMARATE REDUCTASE FROM WOLINELLA SUCCINOGENES

2bs2, resolution 1.78Å

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