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

doi:10.1107/S0907444912012012

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

School of Biochemistry

Research output: Contribution to journal › Article (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 language	English
Pages (from-to)	724-31
Number of pages	8
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	68
Issue number	6
DOIs	https://doi.org/10.1107/S0907444912012012
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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Lunin, V. Y., Lunina, N. L., Casutt, M. S., Knoops, K., Schaffitzel, C., Steuber, J., Fritz, G., & Baumstark, M. W. (2012). Low-resolution structure determination of Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae by ab initio phasing and electron microscopy. Acta Crystallographica Section D: Biological Crystallography, 68(6), 724-31. https://doi.org/10.1107/S0907444912012012

Lunin, Vladimir Y ; Lunina, Natalia L ; Casutt, Marco S ; Knoops, Kèvin ; Schaffitzel, Christiane ; Steuber, Julia ; Fritz, Günter ; Baumstark, Manfred W. / Low-resolution structure determination of Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae by ab initio phasing and electron microscopy. In: Acta Crystallographica Section D: Biological Crystallography. 2012 ; Vol. 68, No. 6. pp. 724-31.

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

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 {\AA} 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.",

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

author = "Lunin, {Vladimir Y} and Lunina, {Natalia L} and Casutt, {Marco S} and K{\`e}vin Knoops and Christiane Schaffitzel and Julia Steuber and G{\"u}nter Fritz and Baumstark, {Manfred W}",

year = "2012",

month = jun,

doi = "10.1107/S0907444912012012",

language = "English",

volume = "68",

pages = "724--31",

journal = "Acta Crystallographica Section D: Biological Crystallography",

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Lunin, VY, Lunina, NL, Casutt, MS, Knoops, K, Schaffitzel, C, Steuber, J, Fritz, G & Baumstark, MW 2012, 'Low-resolution structure determination of Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae by ab initio phasing and electron microscopy', Acta Crystallographica Section D: Biological Crystallography, vol. 68, no. 6, pp. 724-31. https://doi.org/10.1107/S0907444912012012

Low-resolution structure determination of Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae by ab initio phasing and electron microscopy. / Lunin, Vladimir Y; Lunina, Natalia L; Casutt, Marco S; Knoops, Kèvin; Schaffitzel, Christiane; Steuber, Julia; Fritz, Günter; Baumstark, Manfred W.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 68, No. 6, 06.2012, p. 724-31.

Research output: Contribution to journal › Article (Academic Journal)

TY - JOUR

T1 - Low-resolution structure determination of Na(+)-translocating NADH:ubiquinone oxidoreductase from Vibrio cholerae by ab initio phasing and electron microscopy

AU - Lunin, Vladimir Y

AU - Lunina, Natalia L

AU - Casutt, Marco S

AU - Knoops, Kèvin

AU - Schaffitzel, Christiane

AU - Steuber, Julia

AU - Fritz, Günter

AU - Baumstark, Manfred W

PY - 2012/6

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N2 - 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.

AB - 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.

KW - Computational Biology

KW - Electron Transport Complex I

KW - Microscopy, Electron

KW - Models, Molecular

KW - Protein Structure, Tertiary

KW - Structural Homology, Protein

KW - Vibrio cholerae

U2 - 10.1107/S0907444912012012

DO - 10.1107/S0907444912012012

M3 - Article (Academic Journal)

C2 - 22683795

VL - 68

SP - 724

EP - 731

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

SN - 0907-4449

IS - 6

ER -