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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.

Original publication

DOI

10.1038/sj.emboj.7600859

Type

Journal article

Journal

EMBO J

Publication Date

16/11/2005

Volume

24

Pages

3974 - 3983

Keywords

Amino Acid Sequence, Bacterial Proteins, Crystallography, X-Ray, Holoenzymes, Models, Molecular, Molecular Sequence Data, Protein Structure, Quaternary, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Subunits, Sequence Alignment, Thermus thermophilus, Vacuolar Proton-Translocating ATPases