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-Structure paper
Title | Structural basis for gating mechanism of the human sodium-potassium pump. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 5293, Year 2022 |
Publish date | Sep 8, 2022 |
Authors | Phong T Nguyen / Christine Deisl / Michael Fine / Trevor S Tippetts / Emiko Uchikawa / Xiao-Chen Bai / Beth Levine / |
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 ...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. |
External links | Nat Commun / PubMed:36075933 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.4 - 4.1 Å |
Structure data | EMDB-27164, PDB-8d3u: EMDB-27165, PDB-8d3v: EMDB-27166, PDB-8d3w: EMDB-27167, PDB-8d3x: EMDB-27168, PDB-8d3y: |
Chemicals | ChemComp-ADP: ChemComp-ALF: ChemComp-ACP: ChemComp-MF4: |
Source |
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Keywords | TRANSLOCASE/TRANSPORT PROTEIN / Na/K-ATPase / a3 / b1 / FXYD6 / occluded state / TRANSPORT PROTEIN / TRANSLOCASE-TRANSPORT PROTEIN complex / AMPPCP-bound / cytoplasmic side-open |