Lunin Vladimir Y, Lunina Natalia L, Casutt Marco S, Knoops Kèvin, Schaffitzel Christiane, Steuber Julia, Fritz Günter, Baumstark Manfred W
Department of Rehabilitative and Preventative Sports Medicine, University of Freiburg, Hugstetter Strasse 55, 79106 Freiburg, Germany.
Acta Crystallogr D Biol Crystallogr. 2012 Jun;68(Pt 6):724-31. doi: 10.1107/S0907444912012012. Epub 2012 May 17.
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.
通过从头计算相位法确定了来自人类病原体霍乱弧菌的Na(+)-转运NADH：泛醌氧化还原酶的低分辨率结构，并通过电子显微镜独立证实。这种多亚基膜蛋白复合物（分子量210 kDa）产生Na(+)梯度，该梯度对于底物摄取、运动性、致病性和抗生素外排至关重要。获得的16 Å分辨率电子密度图揭示了一个不对称颗粒，其中心区域电子密度低且有一个假定的去污剂区域，并允许识别该复合物的跨膜区域。
