- EMDB-33602: Cryo-EM structure of the Na+,K+-ATPase in the E2.2K+ state after ... -
+
データを開く
IDまたはキーワード:
読み込み中...
-
基本情報
登録情報
データベース: EMDB / ID: EMD-33602
タイトル
Cryo-EM structure of the Na+,K+-ATPase in the E2.2K+ state after addition of ATP
マップデータ
試料
複合体: Sodium/potassium-transporting ATPase
タンパク質・ペプチド: Na, K-ATPase alpha subunit
タンパク質・ペプチド: Na+,K+-ATPase beta subunit
タンパク質・ペプチド: FXYD domain-containing ion transport regulator
リガンド: ADENOSINE-5'-TRIPHOSPHATE
リガンド: POTASSIUM ION
リガンド: CHOLESTEROL
リガンド: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
リガンド: water
機能・相同性
機能・相同性情報
regulation of monoatomic ion transport / P-type sodium:potassium-exchanging transporter activity / sodium:potassium-exchanging ATPase complex / sodium ion export across plasma membrane / intracellular potassium ion homeostasis / intracellular sodium ion homeostasis / potassium ion import across plasma membrane / ATPase activator activity / sodium channel regulator activity / monoatomic ion transport ...regulation of monoatomic ion transport / P-type sodium:potassium-exchanging transporter activity / sodium:potassium-exchanging ATPase complex / sodium ion export across plasma membrane / intracellular potassium ion homeostasis / intracellular sodium ion homeostasis / potassium ion import across plasma membrane / ATPase activator activity / sodium channel regulator activity / monoatomic ion transport / proton transmembrane transport / sarcolemma / ATP hydrolysis activity / ATP binding / membrane / metal ion binding 類似検索 - 分子機能
ジャーナル: FEBS Lett / 年: 2022 タイトル: Cryo-electron microscopy of Na ,K -ATPase reveals how the extracellular gate locks in the E2·2K state. 著者: Ryuta Kanai / Flemming Cornelius / Bente Vilsen / Chikashi Toyoshima / 要旨: 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 ...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.