7Y45

Cryo-EM structure of the Na+,K+-ATPase in the E2.2K+ state

7Y45 の概要

• エントリーDOI: 10.2210/pdb7y45/pdb
• 関連するPDBエントリー: 7Y46
• EMDBエントリー: 33601
• 分子名称: Na, K-ATPase alpha subunit, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, Na+,K+-ATPase beta subunit, ... (11 entities in total)
• 機能のキーワード: na+, k+-atpase, membrane protein, ion transport, transport protein
• 由来する生物種: Squalus acanthias (spiny dogfish); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 348137.10

構造登録者

Kanai, R.,Cornelius, F.,Vilsen, B.,Toyoshima, C. (登録日: 2022-06-14, 公開日: 2022-07-13, 最終更新日: 2024-10-30)

主引用文献

Kanai, R.,Cornelius, F.,Vilsen, B.,Toyoshima, C.
Cryo-electron microscopy of Na + ,K + -ATPase reveals how the extracellular gate locks in the E2·2K + state.
Febs Lett., 596:2513-2524, 2022

PubMed Abstract: Na ,K -ATPase (NKA) is one of the most important members of the P-type ion-translocating ATPases and plays a pivotal role in establishing electrochemical gradients for Na and K across the cell membrane. Presented here is a 3.3 Å resolution structure of NKA in the E2·2K state solved by cryo-electron microscopy. It is a stable state with two occluded K after transferring three Na into the extracellular medium and releasing inorganic phosphate bound to the cytoplasmic P domain. We describe how the extracellular ion pathway wide open in the E2P state becomes closed and locked in E2·2K , linked to events at the phosphorylation site more than 50 Å away. We also show, although at low resolution, how ATP binding to NKA in E2·2K relaxes the gating machinery and thereby accelerates the transition into the next step, that is, the release of K into the cytoplasm, more than 100 times.

PubMed: 35747985
DOI: 10.1002/1873-3468.14437

実験手法

ELECTRON MICROSCOPY (3.3 Å)