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

DOI: 10.1038/nature14003 DOI Help

Authors: Julia Steuber (University of Hohenheim) , Georg Vohl (University of Freiburg) , Marco S. Casutt (University of Freiburg) , Thomas Vorburger (University of Hohenheim) , Kay Diederichs (University of Konstanz) , Guenter Fritz (University of Freiburg)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature , VOL 516 (7529) , PAGES 62 - 67

State: Published (Approved)
Published: December 2014
Diamond Proposal Number(s): 9694 , 10210 , 12090

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.

Diamond Keywords: Bacteria

Subject Areas: Biology and Bio-materials, Chemistry, Medicine


Instruments: I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Other Facilities: X06SA, X06DA at SLS

Added On: 11/02/2015 20:33

Discipline Tags:

Pathogens Antibiotic Resistance Infectious Diseases Health & Wellbeing Biochemistry Chemistry Structural biology Drug Discovery Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)