Crystal structure of the sodium–potassium pump

J. Preben Morth, Bjørn P. Pedersen, Mads S. Toustrup-Jensen, Thomas L.-M. Sørensen, Janne Petersen, Jens Peter Andersen, Bente Vilsen () and Poul Nissen ()
Additional contact information
J. Preben Morth: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Bjørn P. Pedersen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Mads S. Toustrup-Jensen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Thomas L.-M. Sørensen: University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus C, Denmark
Janne Petersen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Jens Peter Andersen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Bente Vilsen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,
Poul Nissen: Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, and,

Nature, 2007, vol. 450, issue 7172, 1043-1049

Abstract: Abstract The Na+,K+-ATPase generates electrochemical gradients for sodium and potassium that are vital to animal cells, exchanging three sodium ions for two potassium ions across the plasma membrane during each cycle of ATP hydrolysis. Here we present the X-ray crystal structure at 3.5 Å resolution of the pig renal Na+,K+-ATPase with two rubidium ions bound (as potassium congeners) in an occluded state in the transmembrane part of the α-subunit. Several of the residues forming the cavity for rubidium/potassium occlusion in the Na+,K+-ATPase are homologous to those binding calcium in the Ca2+-ATPase of sarco(endo)plasmic reticulum. The β- and γ-subunits specific to the Na+,K+-ATPase are associated with transmembrane helices αM7/αM10 and αM9, respectively. The γ-subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the α-subunit is contained within a pocket between transmembrane helices and seems to be a novel regulatory element controlling sodium affinity, possibly influenced by the membrane potential.

Date: 2007
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DOI: 10.1038/nature06419

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