The rotor in the membrane of the ATP synthase and relatives

被引：26

作者：

Arechaga, I ^{[1
]}

Jones, PC ^{[1
]}

机构：

[1] MRC, Dunn Human Nutr Unit, Cambridge CB2 2XY, England

来源：

FEBS LETTERS | 2001年 / 494卷 / 1-2期

关键词：

ATP synthase; subunit c; proton stoichiometry; sequence alignment;

D O I：

10.1016/S0014-5793(01)02300-6

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：

In recent years, structural information on the Fl sector of the ATP synthase has provided an insight into the molecular mechanism of ATP catalysis, The structure strongly supports the proposal that the ATP synthase works as a rotary molecular motor. Insights into the membrane domain have just started to emerge but more detailed structural information is needed if the molecular mechanism of proton translocation coupled to ATP synthesis is to be understood. This review will focus mainly on the ion translocating rotor in the membrane domain of the F-type ATPase, and the related vacuolar and archaeal relatives. (C) 2001 Published by Elsevier Science B,V, on behalf of the Federation of European Biochemical Societies.

引用

页码：1 / 5

页数：5

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