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

ABSTRACT: The crystal structure of subunit F of vacuole-type ATPase/synthase (prokaryotic V-ATPase) was determined to of 2.2 A 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 crosslinking 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.

SUBMITTER: Makyio H

PROVIDER: S-EPMC1283957 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature

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

Makyio Hisayoshi H Iino Ryota R Ikeda Chiyo C Imamura Hiromi H Tamakoshi Masatada M Iwata Momi M Stock Daniela D Bernal Ricardo A RA Carpenter Elisabeth P EP Yoshida Masasuke M Yokoyama Ken K Iwata So S

The EMBO journal 20051110 22

The crystal structure of subunit F of vacuole-type ATPase/synthase (prokaryotic V-ATPase) was determined to of 2.2 A 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 crosslinking experiments. The crystal structure, together with ...[more]

PMID: 16281059

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