7UWA
Citrus V-ATPase State 1, H in contact with subunits AB
This is a non-PDB format compatible entry.
Summary for 7UWA
| Entry DOI | 10.2210/pdb7uwa/pdb |
| EMDB information | 26826 |
| Descriptor | V-type proton ATPase catalytic subunit A, V-type proton ATPase subunit E, V-type proton ATPase subunit G, ... (15 entities in total) |
| Functional Keywords | v-atpase, rotary atpase, complex, membrane protein |
| Biological source | Citrus limon More |
| Total number of polymer chains | 31 |
| Total formula weight | 937231.60 |
| Authors | Abdelaziz, R.A.,Keon, K.A.,Schulze, W.X.,Schumacher, K.,Rubinstein, J.L. (deposition date: 2022-05-03, release date: 2022-07-06, Last modification date: 2024-06-12) |
| Primary citation | Tan, Y.Z.,Keon, K.A.,Abdelaziz, R.,Imming, P.,Schulze, W.,Schumacher, K.,Rubinstein, J.L. Structure of V-ATPase from citrus fruit. Structure, 30:1403-, 2022 Cited by PubMed Abstract: We used the Legionella pneumophila effector SidK to affinity purify the endogenous vacuolar-type ATPases (V-ATPases) from lemon fruit. The preparation was sufficient for cryoelectron microscopy, allowing structure determination of the enzyme in two rotational states. The structure defines the ATP:H ratio of the enzyme, demonstrating that it can establish a maximum ΔpH of ∼3, which is insufficient to maintain the low pH observed in the vacuoles of juice sac cells in lemons and other citrus fruit. Compared with yeast and mammalian enzymes, the membrane region of the plant V-ATPase lacks subunit f and possesses an unusual configuration of transmembrane α helices. Subunit H, which inhibits ATP hydrolysis in the isolated catalytic region of V-ATPase, adopts two different conformations in the intact complex, hinting at a role in modulating activity in the intact enzyme. PubMed: 36041457DOI: 10.1016/j.str.2022.07.006 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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