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-Structure paper
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. |
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ジャーナル・号・ページ | FEBS Lett, Vol. 597, Issue 15, Page 1957-1976, Year 2023 |
掲載日 | 2023年6月26日 |
著者 | Ryuta Kanai / Bente Vilsen / Flemming Cornelius / Chikashi Toyoshima / |
PubMed 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. |
リンク | FEBS Lett / PubMed:37357620 |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.8 - 3.5 Å |
構造データ | EMDB-36220, PDB-8jfz: PDB-8jbk: PDB-8jbl: PDB-8jbm: |
化合物 | ChemComp-MN: ChemComp-NA: ChemComp-CLR: ChemComp-PC1: ChemComp-PCW: ChemComp-NAG: ChemComp-DMU: ChemComp-HOH: ChemComp-MG: |
由来 |
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キーワード | MEMBRANE PROTEIN (膜タンパク質) / ion pump / P-type ATPase |