IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v516y2014i7529d10.1038_nature14003.html
   My bibliography  Save this article

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

Author

Listed:
  • Julia Steuber

    (Garbenstrasse 30, University of Hohenheim, 70599 Stuttgart, Germany)

  • Georg Vohl

    (Institute for Neuropathology, University of Freiburg, Breisacher Strasse 64, 79106 Freiburg, Germany
    Hermann-Staudinger-Graduate school, University of Freiburg, Hebelstrasse 27, 79104 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)

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.

Suggested Citation

  • Julia Steuber & Georg Vohl & Marco S. Casutt & Thomas Vorburger & Kay Diederichs & Günter Fritz, 2014. "Structure of the V. cholerae Na+-pumping NADH:quinone oxidoreductase," Nature, Nature, vol. 516(7529), pages 62-67, December.
    • Handle: RePEc:nat:nature:v:516:y:2014:i:7529:d:10.1038_nature14003
    DOI: 10.1038/nature14003
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature14003
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature14003?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Stella Vitt & Simone Prinz & Martin Eisinger & Ulrich Ermler & Wolfgang Buckel, 2022. "Purification and structural characterization of the Na+-translocating ferredoxin: NAD+ reductase (Rnf) complex of Clostridium tetanomorphum," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Jun-ichi Kishikawa & Moe Ishikawa & Takahiro Masuya & Masatoshi Murai & Yuki Kitazumi & Nicole L. Butler & Takayuki Kato & Blanca Barquera & Hideto Miyoshi, 2022. "Cryo-EM structures of Na+-pumping NADH-ubiquinone oxidoreductase from Vibrio cholerae," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:516:y:2014:i:7529:d:10.1038_nature14003. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.