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Low-resolution structure determination of Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae by ab initio phasing and electron microscopy

  • Vladimir Y Lunin
  • , Natalia L Lunina
  • , Marco S Casutt
  • , Kèvin Knoops
  • , Christiane Schaffitzel
  • , Julia Steuber
  • , Günter Fritz
  • , Manfred W Baumstark

    Research output: Contribution to journalArticle (Academic Journal)peer-review

    5 Citations (Scopus)

    Abstract

    A low-resolution structure of the Na(+)-translocating NADH:ubiquinone oxidoreductase from the human pathogen Vibrio cholerae was determined by ab initio phasing and independently confirmed by electron microscopy. This multi-subunit membrane-protein complex (molecular weight 210 kDa) generates an Na(+) gradient that is essential for substrate uptake, motility, pathogenicity and efflux of antibiotics. The obtained 16 Å resolution electron density-map revealed an asymmetric particle with a central region of low electron density and a putative detergent region, and allowed the identification of the transmembrane regions of the complex.

    Original languageEnglish
    Pages (from-to)724-31
    Number of pages8
    JournalActa Crystallographica Section D: Biological Crystallography
    Volume68
    Issue number6
    DOIs
    Publication statusPublished - Jun 2012

    Keywords

    • Computational Biology
    • Electron Transport Complex I
    • Microscopy, Electron
    • Models, Molecular
    • Protein Structure, Tertiary
    • Structural Homology, Protein
    • Vibrio cholerae

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