ATP synthase - the structure of the stator stalk

被引：33

作者：

Weber, Joachim ^{[1
]}

机构：

[1] Texas Tech Univ, Dept Chem & Biochem, Lubbock, TX 79409 USA

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2007年 / 32卷 / 02期

关键词：

D O I：

10.1016/j.tibs.2006.12.006

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：

ATP synthase synthesizes ATP from ADP and inorganic phosphate using a unique rotary mechanism whereby two subcomplexes move relative to each other, powered by a proton or sodium gradient. The non-rotating parts of the machinery are held together by the 'stator stalk'. The recent resolution of the structure of a major portion of the stator stalk of mitochondrial ATP synthase represents an important step towards a structural model for the ATP synthase holoenzyme.

引用

页码：53 / 56

页数：4

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