7X24

Cryo-EM structure of non gastric H,K-ATPase alpha2 SPWC mutant in (2K+)E2-AlF state

7X24 の概要

• エントリーDOI: 10.2210/pdb7x24/pdb
• EMDBエントリー: 32957
• 分子名称: Potassium-transporting ATPase alpha chain 2, Sodium/potassium-transporting ATPase subunit beta-1, POTASSIUM ION, ... (8 entities in total)
• 機能のキーワード: p-type atpase, transporter, proton pump, kidney, colon, airway, membrane protein
• 由来する生物種: Rattus norvegicus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 152223.87

構造登録者

Abe, K.,Nakanishi, H.,Young, V.,Artigas, P. (登録日: 2022-02-25, 公開日: 2022-10-05, 最終更新日: 2024-11-20)

主引用文献

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

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: 36085139
DOI: 10.1038/s41467-022-32793-0

実験手法

ELECTRON MICROSCOPY (3.4 Å)