Three-dimensional structure of bovine heart NADH:ubiquinone oxidoreductase (complex I) by electron microscopy of a single negatively stained two-dimensional crystal
Three-dimensional structure of bovine heart NADH:ubiquinone oxidoreductase (complex I) by electron microscopy of a single negatively stained two-dimensional crystal
复制标题
通过电子显微镜观察单个负染二维晶体的牛心 NADH：泛醌氧化还原酶（复合物 I）的三维结构
DOI：
10.1093/jmicro/dft082
复制
发表时间：
2014
期刊：
影响因子：
1.8
通讯作者：
S. Shimada
中科院分区：
文献类型：
--
作者：
井濱 太;山本 麻実;宮田 愛彦;松崎 勝巳;星野 大;S. Shimada
牛心 NADH：泛醌氧化还原酶（复合物 I）是线粒体呼吸链中最大（约 1 MDa）的膜蛋白复合物，催化从 NADH 到泛醌的电子转移，并伴有质子泵送。我们在重建的脂质双层中结晶了牛复合物 I，并通过单个负染色二维晶体的电子晶体学分析获得了三维密度图。尺寸为a= 388 Å、b= 129 Å、γ= 90°的不对称单元包含两个分子，具有P1对称性。两个分子之间的结构差异表明亲水域相对于膜嵌入域的灵活性。
Bovine heart NADH:ubiquinone oxidoreductase (complex I), which is the largest (about 1 MDa) membrane protein complex in the mitochondrial respiratory chain, catalyzes the electron transfer from NADH to ubiquinone, coupled with proton pumping. We have crystallized bovine complex I in reconstituted lipid bilayers and obtained a three-dimensional density map by the electron crystallographic analysis of a single negatively stained two-dimensional crystal. The asymmetric unit with dimensions ofa= 388 Å,b= 129 Å andγ= 90° contains two molecules and is ofP1 symmetry. Structural differences between the two molecules indicate flexibility of the hydrophilic domain relative to the membrane-embedded domain.