7VAQ
V1EG of V/A-ATPase from Thermus thermophilus, high ATP, state3-2
This is a non-PDB format compatible entry.
Summary for 7VAQ
| Entry DOI | 10.2210/pdb7vaq/pdb |
| EMDB information | 31858 |
| Descriptor | V-type ATP synthase alpha chain, ADENOSINE-5'-TRIPHOSPHATE, V-type ATP synthase beta chain, ... (10 entities in total) |
| Functional Keywords | rotary atpase, v-type atpase, atp synthase, thermus thermophilus, chemo-mechanical coupling, motor protein |
| Biological source | Thermus thermophilus HB8 More |
| Total number of polymer chains | 12 |
| Total formula weight | 455887.58 |
| Authors | Kishikawa, J.,Nakanishi, A.,Nakano, A.,Saeki, S.,Furuta, A.,Kato, T.,Mitsuoka, K.,Yokoyama, K. (deposition date: 2021-08-30, release date: 2022-07-13, Last modification date: 2024-06-19) |
| Primary citation | Kishikawa, J.,Nakanishi, A.,Nakano, A.,Saeki, S.,Furuta, A.,Kato, T.,Mistuoka, K.,Yokoyama, K. Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases. Nat Commun, 13:1213-1213, 2022 Cited by PubMed Abstract: V/A-ATPase is a motor protein that shares a common rotary catalytic mechanism with FF ATP synthase. When powered by ATP hydrolysis, the V domain rotates the central rotor against the AB hexamer, composed of three catalytic AB dimers adopting different conformations (AB, AB, and AB). Here, we report the atomic models of 18 catalytic intermediates of the V domain of V/A-ATPase under different reaction conditions, determined by single particle cryo-EM. The models reveal that the rotor does not rotate immediately after binding of ATP to the V. Instead, three events proceed simultaneously with the 120˚ rotation of the shaft: hydrolysis of ATP in AB, zipper movement in AB by the binding ATP, and unzipper movement in AB with release of both ADP and Pi. This indicates the unidirectional rotation of V/A-ATPase by a ratchet-like mechanism owing to ATP hydrolysis in AB, rather than the power stroke model proposed previously for F-ATPase. PubMed: 35260556DOI: 10.1038/s41467-022-28832-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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