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)

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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