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Significance This study explores the structural basis for the difference between the closely related Na+ ,K+ -ATPase and H+ ,K+ -ATPase with respect to ion transport stoichiometry, electrogenicity, and cation selectivity, which has long been an enigma. A cysteine in the membrane domain of Na+ ,K+ -ATPase is substituted by arginine in H+ ,K+ -ATPase and has been found to be replaced by phenylalanine in a patient with alternating hemiplegia of childhood. These substitutions affect the functioning of the Na+ -specific site of Na+ ,K+ -ATPase profoundly. The positively charged side chain of the arginine present in H+ ,K+ -ATPase serves as an internal cation that replaces bound Na+ , thus explaining how H+ ,K+ -ATPase avoids binding and transporting Na+ at this site, thereby performing electroneutral transport, despite the general structural and functional resemblance to the electrogenic Na+ ,K+ -ATPase.

proceedings of the national academy of sciences of the united states of america

Arginine substitution of a cysteine in transmembrane helix M8 converts Na + ,K + -ATPase to an electroneutral pump similar to H + ,K + -ATPase