Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus

被引:48
作者
Makyio, H
Iino, R
Ikeda, C
Imamura, H
Tamakoshi, M
Iwata, M
Stock, D
Bernal, RA
Carpenter, EP
Yoshida, M
Yokoyama, K
Iwata, S
机构
[1] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AZ, England
[2] Japan Sci & Technol Agcy, ATP Syst Project Exploratory Res Adv Technol, Yokohama, Kanagawa, Japan
[3] Tokyo Inst Technol, Chem Resources Lab, Yokohama, Kanagawa 227, Japan
[4] MRC, Mol Biol Lab, Cambridge CB2 2QH, England
[5] Tokyo Univ Pharm & Life Sci, Dept Mol Biol, Tokyo, Japan
基金
英国生物技术与生命科学研究理事会;
关键词
ATP synthase; CheY; crystal structure; rotary motor; V-ATPase;
D O I
10.1038/sj.emboj.7600859
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
The crystal structure of subunit F of vacuole-type ATPase/synthase (prokaryotic V-ATPase) was determined to of 2.2 angstrom resolution. The subunit reveals unexpected structural similarity to the response regulator proteins that include the Escherichia coli chemotaxis response regulator CheY. The structure was successfully placed into the low-resolution EM structure of the prokaryotic holo-V-ATPase at a location indicated by the results of cross-linking experiments. The crystal structure, together with the single-molecule analysis using fluorescence resonance energy transfer, showed that the subunit F exhibits two conformations, a 'retracted' form in the absence and an 'extended' form in the presence of ATP. Our results postulated that the subunit F is a regulatory subunit in the V-ATPase.
引用
收藏
页码:3974 / 3983
页数:10
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