Structural highlights
Function
[VATF_THET8] Produces ATP from ADP in the presence of a proton gradient across the membrane.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus.,Makyio H, Iino R, Ikeda C, Imamura H, Tamakoshi M, Iwata M, Stock D, Bernal RA, Carpenter EP, Yoshida M, Yokoyama K, Iwata S EMBO J. 2005 Nov 16;24(22):3974-83. Epub 2005 Nov 10. PMID:16281059[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Makyio H, Iino R, Ikeda C, Imamura H, Tamakoshi M, Iwata M, Stock D, Bernal RA, Carpenter EP, Yoshida M, Yokoyama K, Iwata S. Structure of a central stalk subunit F of prokaryotic V-type ATPase/synthase from Thermus thermophilus. EMBO J. 2005 Nov 16;24(22):3974-83. Epub 2005 Nov 10. PMID:16281059
