8D3X

Human alpha3 Na+/K+-ATPase in its K+-occluded state

8D3X の概要

• エントリーDOI: 10.2210/pdb8d3x/pdb
• EMDBエントリー: 27167
• 分子名称: Sodium/potassium-transporting ATPase subunit beta-1, FXYD domain-containing ion transport regulator 6, Sodium/potassium-transporting ATPase subunit alpha-3, ... (4 entities in total)
• 機能のキーワード: na/k-atpase, a3, b1, fxyd6, occluded state, transport protein, translocase-transport protein complex, translocase/transport 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: 157928.49

構造登録者

Nguyen, P.T.,Bai, X. (登録日: 2022-06-01, 公開日: 2022-09-21, 最終更新日: 2025-05-28)

主引用文献

Nguyen, P.T.,Deisl, C.,Fine, M.,Tippetts, T.S.,Uchikawa, E.,Bai, X.C.,Levine, B.
Structural basis for gating mechanism of the human sodium-potassium pump.
Nat Commun, 13:5293-5293, 2022

PubMed Abstract: P2-type ATPase sodium-potassium pumps (Na/K-ATPases) are ion-transporting enzymes that use ATP to transport Na and K on opposite sides of the lipid bilayer against their electrochemical gradients to maintain ion concentration gradients across the membranes in all animal cells. Despite the available molecular architecture of the Na/K-ATPases, a complete molecular mechanism by which the Na and K ions access into and are released from the pump remains unknown. Here we report five cryo-electron microscopy (cryo-EM) structures of the human alpha3 Na/K-ATPase in its cytoplasmic side-open (E1), ATP-bound cytoplasmic side-open (E1•ATP), ADP-AlF trapped Na-occluded (E1•P-ADP), BeF trapped exoplasmic side-open (E2P) and MgF trapped K-occluded (E2•P) states. Our work reveals the atomically resolved structural detail of the cytoplasmic gating mechanism of the Na/K-ATPase.

PubMed: 36075933
DOI: 10.1038/s41467-022-32990-x

実験手法

ELECTRON MICROSCOPY (4.1 Å)