7E20

Cryo EM structure of a K+-bound Na+,K+-ATPase in the E2 state

7E20 の概要

• エントリーDOI: 10.2210/pdb7e20/pdb
• EMDBエントリー: 30948
• 分子名称: Sodium/potassium-transporting ATPase subunit alpha-1, Sodium/potassium-transporting ATPase subunit beta-1, Sodium/potassium-transporting ATPase subunit gamma, ... (10 entities in total)
• 機能のキーワード: na+, k+-atpase, membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 159911.12

構造登録者

Guo, Y.Y.,Zhang, Y.Y.,Yan, R.H.,Huang, B.D.,Ye, F.F.,Wu, L.S.,Chi, X.M.,Zhou, Q. (登録日: 2021-02-04, 公開日: 2022-06-15, 最終更新日: 2024-10-16)

主引用文献

Guo, Y.,Zhang, Y.,Yan, R.,Huang, B.,Ye, F.,Wu, L.,Chi, X.,Shi, Y.,Zhou, Q.
Cryo-EM structures of recombinant human sodium-potassium pump determined in three different states.
Nat Commun, 13:3957-3957, 2022

PubMed Abstract: Sodium-Potassium Pump (Na/K-ATPase, NKA) is an ion pump that generates an electrochemical gradient of sodium and potassium ions across the plasma membrane by hydrolyzing ATP. During each Post-Albers cycle, NKA exchanges three cytoplasmic sodium ions for two extracellular potassium ions through alternating changes between the E1 and E2 states. Hitherto, several steps remained unknown during the complete working cycle of NKA. Here, we report cryo-electron microscopy (cryo-EM) structures of recombinant human NKA (hNKA) in three distinct states at 2.7-3.2 Å resolution, representing the E1·3Na and E1·3Na·ATP states with cytosolic gates open and the basic E2·[2K] state, respectively. This work provides the insights into the cytoplasmic Na entrance pathway and the mechanism of cytoplasmic gate closure coupled with ATP hydrolysis, filling crucial gaps in the structural elucidation of the Post-Albers cycle of NKA.

PubMed: 35803952
DOI: 10.1038/s41467-022-31602-y

実験手法

ELECTRON MICROSCOPY (2.7 Å)