7X20
Crystal structure of non gastric H,K-ATPase alpha2 in (K+)E2-AlF state
Summary for 7X20
| Entry DOI | 10.2210/pdb7x20/pdb |
| Descriptor | Potassium-transporting ATPase alpha chain 2, Sodium/potassium-transporting ATPase subunit beta-1, TETRAFLUOROALUMINATE ION, ... (6 entities in total) |
| Functional Keywords | p-type atpase, transporter, proton pump, colon, kidney, airway, membrane protein |
| Biological source | Rattus norvegicus More |
| Total number of polymer chains | 2 |
| Total formula weight | 147003.93 |
| Authors | Nakanishi, H.,Abe, K. (deposition date: 2022-02-25, release date: 2022-10-05, Last modification date: 2024-11-06) |
| Primary citation | Young, V.C.,Nakanishi, H.,Meyer, D.J.,Nishizawa, T.,Oshima, A.,Artigas, P.,Abe, K. Structure and function of H + /K + pump mutants reveal Na + /K + pump mechanisms. Nat Commun, 13:5270-5270, 2022 Cited by PubMed Abstract: Ion-transport mechanisms evolve by changing ion-selectivity, such as switching from Na to H selectivity in secondary-active transporters or P-type-ATPases. Here we study primary-active transport via P-type ATPases using functional and structural analyses to demonstrate that four simultaneous residue substitutions transform the non-gastric H/K pump, a strict H-dependent electroneutral P-type ATPase, into a bona fide Na-dependent electrogenic Na/K pump. Conversion of a H-dependent primary-active transporter into a Na-dependent one provides a prototype for similar studies of ion-transport proteins. Moreover, we solve the structures of the wild-type non-gastric H/K pump, a suitable drug target to treat cystic fibrosis, and of its Na/K pump-mimicking mutant in two major conformations, providing insight on how Na binding drives a concerted mechanism leading to Na/K pump phosphorylation. PubMed: 36085139DOI: 10.1038/s41467-022-32793-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.3 Å) |
Structure validation
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