A cryoelectron microscopy study of the interaction of the Escherichia coli F1‐ATPase with subunit b dimer

FEBS Letters

Capaldi, Roderick A.²  Wilkens, Stephan²  Dunn, Stanley D.¹ 

[1] Department of Biochemistry, University of Western Ontario, London, Ont. N6A 5C1, Canada;Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA

关键词: Cryoelectron microscopy;    F1-ATPase;    ATP synthase;    b subunit;   

DOI  :  10.1016/0014-5793(94)01059-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A complex between the Escherichia coli F₁-ATPase and a truncated form of the ECF₀-b subunit was formed and examined by cryoelectron microscopy in amorphous ice. Image analysis of single particles in the hexagonal projection revealed that the polar domain of the b subunit interacts with a β subunit different from the one which interacts with the ϵ subunit. The cavity in the enzyme, visible in the hexagonal projection, is not filled by the b polypeptide, therefore leaving enough room for extensive conformational changes of the γ and ϵ subunits within the native F₁F₀ complex.

【 授权许可】

Unknown