Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase


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STEUBER, Julia, Georg VOHL, Marco S. CASUTT, Kay DIEDERICHS, Günter FRITZ, 2014. Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase. In: Nature. 516(7529), pp. 62-67. ISSN 0028-0836. eISSN 1476-4687. Available under: doi: 10.1038/nature14003

@article{Steuber2014Struc-29488, title={Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase}, year={2014}, doi={10.1038/nature14003}, number={7529}, volume={516}, issn={0028-0836}, journal={Nature}, pages={62--67}, author={Steuber, Julia and Vohl, Georg and Casutt, Marco S. and Diederichs, Kay and Fritz, Günter} }

Steuber, Julia Structure of the V. cholerae Na<sup>+</sup>-pumping NADH:quinone oxidoreductase Diederichs, Kay Vohl, Georg 2014 eng Diederichs, Kay Casutt, Marco S. Casutt, Marco S. Fritz, Günter Vohl, Georg 2015-01-12T09:22:14Z Steuber, Julia 2015-01-12T09:22:14Z 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<sup>+</sup>-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<sup>+</sup>-NQR complex has been available until now. Here we present the crystal structure of the Na<sup>+</sup>-NQR complex at 3.5 Å 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<sup>+</sup>-NQR and is structurally related to urea and ammonia transporters. On the basis of the structure we propose a mechanism of redox-driven Na<sup>+</sup> translocation where the change in redox state of the flavin mononucleotide cofactor in NqrB triggers the transport of Na<sup>+</sup> through the observed channel. Fritz, Günter

Dateiabrufe seit 12.01.2015 (Informationen über die Zugriffsstatistik)

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