Cryo-EM Structure of the Yeast ATP Synthase

被引:45
作者
Lau, Wilson C. Y.
Baker, Lindsay A.
Rubinstein, John L.
机构
[1] Hosp Sick Children, Res Inst, Mol Struct & Funct Program, Toronto, ON M5G 1X8, Canada
[2] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A1, Canada
基金
加拿大健康研究院; 加拿大自然科学与工程研究理事会;
关键词
ATP synthase; structure; Saccharomyces cerevisiae; cryo-EM; single particle;
D O I
10.1016/j.jmb.2008.08.014
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
We have used electron cryomicroscopy of single particles to determine the structure of the ATP synthase from Saccharomyces cerevisiae. The resulting map at 24 angstrom resolution can accommodate atomic models of the F-1-c(10) subcomplex, the peripheral stalk subcomplex, and the N-terminal domain of the oligomycin sensitivity conferral protein. The map is similar to an earlier electron cryomicroscopy structure of bovine mitochondrial ATP synthase but with important differences. It resolves the internal structure of the membrane region of the complex, especially the membrane embedded Subunits b, c, and a. Comparison of the yeast ATP synthase map, which lacks density from the dimer-specific subunits e and g, with a map of the bovine enzyme that included e and g indicates where these subunits are located in the intact complex. This new map has allowed construction of a model Of subunit arrangement in the F-O motor of ATP synthase that dictates how dimerization of the complex via subunits e and g might occur. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:1256 / 1264
页数:9
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