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 language | English |
|---|---|
| Pages (from-to) | 724-31 |
| Number of pages | 8 |
| Journal | Acta Crystallographica Section D: Biological Crystallography |
| Volume | 68 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 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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