Crystallization of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae
Crystallization of the Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae
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DOI：
10.1107/s1744309110043125
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发表时间：
2010-12-01
影响因子：
0.9
通讯作者：
Fritz, Guenter
中科院分区：
文献类型：
--
作者：
Casutt, Marco S.;Wendelspiess, Severin;Fritz, Guenter
来自人类病原体霍乱弧菌的Na+-易位NADH：醌氧化还原酶（Na+-NQR）通过膜结合的醌与Na+跨膜易位偶联NADH的放能氧化。Na+-NQR由六个不同的亚基（NqrA-NqrF）组成，并含有一个[2Fe-2S]簇、一个非共价结合的FAD、一个非共价结合的核黄素、两个共价结合的FMNs和可能作为辅因子的Q（8）。整个Na+-NQR复合物的初始结晶通过使用纳升分配器的坐滴法实现。结晶条件的优化产生了平坦的黄色晶体，尺寸高达200 × 80 × 20 μ m。晶体衍射至4.0 A分辨率，属于空间群P2（1），晶胞参数a = 94，B = 146，c = 105 A，α = γ = 90，β = 111度。
The Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) from the human pathogen Vibrio cholerae couples the exergonic oxidation of NADH by membrane-bound quinone to Na+ translocation across the membrane. Na+-NQR consists of six different subunits (NqrA-NqrF) and contains a [2Fe-2S] cluster, a noncovalently bound FAD, a noncovalently bound riboflavin, two covalently bound FMNs and potentially Q(8) as cofactors. Initial crystallization of the entire Na+-NQR complex was achieved by the sitting-drop method using a nanolitre dispenser. Optimization of the crystallization conditions yielded flat yellow-coloured crystals with dimensions of up to 200 x 80 x 20 mu m. The crystals diffracted to 4.0 A resolution and belonged to space group P2(1), with unit-cell parameters a = 94, b = 146, c = 105 A, alpha = gamma = 90, beta = 111 degrees.