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4p6v

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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=4p6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p6v RCSB], [http://www.ebi.ac.uk/pdbsum/4p6v PDBsum]</span></td></tr>
<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=4p6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p6v RCSB], [http://www.ebi.ac.uk/pdbsum/4p6v PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/NQRF_VIBCH NQRF_VIBCH]] NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway. [[http://www.uniprot.org/uniprot/NQRD_VIBCH NQRD_VIBCH]] NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. [[http://www.uniprot.org/uniprot/NQRA_VIBCH NQRA_VIBCH]] NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. [[http://www.uniprot.org/uniprot/NQRC_VIBCH NQRC_VIBCH]] NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol (By similarity). [[http://www.uniprot.org/uniprot/NQRB_VIBCH NQRB_VIBCH]] NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. [[http://www.uniprot.org/uniprot/NQRE_VIBCH NQRE_VIBCH]] NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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NADH oxidation in the respiratory chain is coupled to ion translocation across the membrane to build up an electrochemical gradient. The sodium-translocating NADH:quinone oxidoreductase (Na(+)-NQR), a membrane protein complex widespread among pathogenic bacteria, consists of six subunits, NqrA, B, C, D, E and F. To our knowledge, no structural information on the Na(+)-NQR complex has been available until now. Here we present the crystal structure of the Na(+)-NQR complex at 3.5 A resolution. The arrangement of cofactors both at the cytoplasmic and the periplasmic side of the complex, together with a hitherto unknown iron centre in the midst of the membrane-embedded part, reveals an electron transfer pathway from the NADH-oxidizing cytoplasmic NqrF subunit across the membrane to the periplasmic NqrC, and back to the quinone reduction site on NqrA located in the cytoplasm. A sodium channel was localized in subunit NqrB, which represents the largest membrane subunit of the Na(+)-NQR and is structurally related to urea and ammonia transporters. On the basis of the structure we propose a mechanism of redox-driven Na(+) translocation where the change in redox state of the flavin mononucleotide cofactor in NqrB triggers the transport of Na(+) through the observed channel.
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Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase.,Steuber J, Vohl G, Casutt MS, Vorburger T, Diederichs K, Fritz G Nature. 2014 Dec 4;516(7529):62-7. doi: 10.1038/nature14003. PMID:25471880<ref>PMID:25471880</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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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 10:49, 24 December 2014

Crystal structure of the Na+-translocating NADH: ubiquinone oxidoreductase from Vibrio cholerae

4p6v, resolution 3.50Å

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