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Crystal structure of the sodium-potassium pump.

Nature (2007-12-14)
J Preben Morth, Bjørn P Pedersen, Mads S Toustrup-Jensen, Thomas L-M Sørensen, Janne Petersen, Jens Peter Andersen, Bente Vilsen, Poul Nissen
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 A 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 alpha-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 beta- and gamma-subunits specific to the Na+,K+-ATPase are associated with transmembrane helices alphaM7/alphaM10 and alphaM9, respectively. The gamma-subunit corresponds to a fragment of the V-type ATPase c subunit. The carboxy terminus of the alpha-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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Magnesium fluoride, technical grade
Sigma-Aldrich
Magnesium fluoride, random crystals, optical grade, ≥99.99% trace metals basis
Sigma-Aldrich
Magnesium fluoride, pieces, 3-6 mm, 99.9% trace metals basis (excluding Na)