Low-resolution structure determination of Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae by ab initio phasing and electron microscopy.
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.
Department of Rehabilitative and Preventative Sports Medicine, University of Freiburg, Hugstetter Strasse 55, 79106 Freiburg, Germany.
Vladimir Y
VY
Lunin
Natalia L
NL
Lunina
Marco S
MS
Casutt
Kèvin
K
Knoops
Christiane
C
Schaffitzel
Julia
J
Steuber
Günter
G
Fritz
Manfred W
MW
Baumstark
D019295:Computational Biology; D042967:Electron Transport Complex I / Q000737:chemistry*; D008854:Microscopy, Electron; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein; D014734:Vibrio cholerae / Q000201:enzymology*
D042967:Electron Transport Complex I