The rotor in the membrane of the ATP synthase and relatives

FEBS Letters

Jones, Phil C¹  Arechaga, Ignacio¹ 

[1] The Medical Research Council Dunn Human Nutrition Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, UK

关键词: ATP synthase;    Subunit c;    Proton stoichiometry;    Sequence alignment;   

DOI  :  10.1016/S0014-5793(01)02300-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In recent years, structural information on the F₁ 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.

【 授权许可】

Unknown