8D3Y

Human alpha3 Na+/K+-ATPase in its exoplasmic side-open state

Summary for 8D3Y

• Entry DOI: 10.2210/pdb8d3y/pdb
• EMDB information: 27168
• Descriptor: Sodium/potassium-transporting ATPase subunit alpha-3, Sodium/potassium-transporting ATPase subunit beta-1, FXYD domain-containing ion transport regulator 6 (3 entities in total)
• Functional Keywords: na/k-atpase, a3, b1, fxyd6, occluded state, transport protein, translocase-transport protein complex, translocase/transport protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 3
• Total formula weight: 157689.10

Authors

Nguyen, P.T.,Bai, X. (deposition date: 2022-06-01, release date: 2022-09-21, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.9 Å)