Structural basis for gating mechanism of the human sodium-potassium pump

Phong T. Nguyen (), Christine Deisl, Michael Fine, Trevor S. Tippetts, Emiko Uchikawa, Xiao-chen Bai () and Beth Levine
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Phong T. Nguyen: University of Texas Southwestern Medical Center
Christine Deisl: University of Texas Southwestern Medical Center
Michael Fine: University of Texas Southwestern Medical Center
Trevor S. Tippetts: University of Texas Southwestern Medical Center
Emiko Uchikawa: University of Texas Southwestern Medical Center
Xiao-chen Bai: University of Texas Southwestern Medical Center
Beth Levine: University of Texas Southwestern Medical Center

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: 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-AlF4− trapped Na+-occluded (E1•P-ADP), BeF3− trapped exoplasmic side-open (E2P) and MgF42− trapped K+-occluded (E2•Pi) states. Our work reveals the atomically resolved structural detail of the cytoplasmic gating mechanism of the Na+/K+-ATPase.

Date: 2022
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DOI: 10.1038/s41467-022-32990-x

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