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

Julia Steuber, Georg Vohl, Marco S. Casutt, Thomas Vorburger, Kay Diederichs and Günter Fritz ()
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Julia Steuber: Garbenstrasse 30, University of Hohenheim, 70599 Stuttgart, Germany
Georg Vohl: Institute for Neuropathology, University of Freiburg, Breisacher Strasse 64, 79106 Freiburg, Germany
Marco S. Casutt: Institute for Neuropathology, University of Freiburg, Breisacher Strasse 64, 79106 Freiburg, Germany
Thomas Vorburger: Garbenstrasse 30, University of Hohenheim, 70599 Stuttgart, Germany
Kay Diederichs: University of Konstanz, Universitätsstrasse 10, 78457 Konstanz, Germany
Günter Fritz: Institute for Neuropathology, University of Freiburg, Breisacher Strasse 64, 79106 Freiburg, Germany

Nature, 2014, vol. 516, issue 7529, 62-67

Abstract: Abstract 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 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+-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.

Date: 2014
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DOI: 10.1038/nature14003

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