- EMDB-36220: Cryo-EM structure of Na+,K+-ATPase in the E1.Mg2+ state. -
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基本情報
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データベース: EMDB / ID: EMD-36220
タイトル
Cryo-EM structure of Na+,K+-ATPase in the E1.Mg2+ state.
マップデータ
試料
複合体: Na+,K+-ATPase
タンパク質・ペプチド: Na+,K+-ATPase beta subunit
タンパク質・ペプチド: Na, K-ATPase alpha subunit
タンパク質・ペプチド: FXYD domain-containing ion transport regulator
リガンド: CHOLESTEROL
リガンド: 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE
リガンド: MAGNESIUM ION
リガンド: water
キーワード
ion pump / P-type ATPase / MEMBRANE PROTEIN
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: 2023 タイトル: Crystal structures of Na ,K -ATPase reveal the mechanism that converts the K -bound form to Na -bound form and opens and closes the cytoplasmic gate. 著者: Ryuta Kanai / Bente Vilsen / Flemming Cornelius / Chikashi Toyoshima / 要旨: Na ,K -ATPase (NKA) plays a pivotal role in establishing electrochemical gradients for Na and K across the cell membrane by alternating between the E1 (showing high affinity for Na and low affinity ...Na ,K -ATPase (NKA) plays a pivotal role in establishing electrochemical gradients for Na and K across the cell membrane by alternating between the E1 (showing high affinity for Na and low affinity for K ) and E2 (low affinity to Na and high affinity to K ) forms. Presented here are two crystal structures of NKA in E1·Mg and E1·3Na states at 2.9 and 2.8 Å resolution, respectively. These two E1 structures fill a gap in our description of the NKA reaction cycle based on the atomic structures. We describe how NKA converts the K -bound E2·2K form to an E1 (E1·Mg ) form, which allows high-affinity Na binding, eventually closing the cytoplasmic gate (in E1 ~ P·ADP·3Na ) after binding three Na , while keeping the extracellular ion pathway sealed. We now understand previously unknown functional roles for several parts of NKA and that NKA uses even the lipid bilayer for gating the ion pathway.