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2D00

Subunit F of V-type ATPase/synthase

Summary for 2D00
Entry DOI10.2210/pdb2d00/pdb
DescriptorV-type ATP synthase subunit F, CALCIUM ION (3 entities in total)
Functional Keywordsv-atpase, subunit f, chey, fret, hydrolase
Biological sourceThermus thermophilus
Total number of polymer chains6
Total formula weight71432.33
Authors
Makyio, H.,Iino, R.,Ikeda, C.,Imamura, H.,Tamakoshi, M.,Iwata, M.,Stock, D.,Bernal, R.A.,Carpenter, E.P.,Yoshida, M.,Yokoyama, K.,Iwata, S. (deposition date: 2005-07-21, release date: 2005-12-06, Last modification date: 2024-03-13)
Primary citationMakyio, H.,Iino, R.,Ikeda, C.,Imamura, H.,Tamakoshi, M.,Iwata, M.,Stock, D.,Bernal, R.A.,Carpenter, E.P.,Yoshida, M.,Yokoyama, K.,Iwata, S.
Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus
Embo J., 24:3974-3983, 2005
Cited by
PubMed 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.
PubMed: 16281059
DOI: 10.1038/sj.emboj.7600859
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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