2D00
Subunit F of V-type ATPase/synthase
Summary for 2D00
Entry DOI | 10.2210/pdb2d00/pdb |
Descriptor | V-type ATP synthase subunit F, CALCIUM ION (3 entities in total) |
Functional Keywords | v-atpase, subunit f, chey, fret, hydrolase |
Biological source | Thermus thermophilus |
Total number of polymer chains | 6 |
Total formula weight | 71432.33 |
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 citation | 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. 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: 16281059DOI: 10.1038/sj.emboj.7600859 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report