Structure and action of the Na+ /K+ -ATPase
The Na+ /K+ -ATPase is an integral membrane protein consisting of α55 kDa β and 110 kDa subunits. The functional unit is either a heterotetramer (α2β2) or, more likely, a heterodimer. Upon hydrolysis of one molecule of ATP to ADP and Pi the Pi transiently binds to an aspartyl residue in the protein, the protein undergoes a conformational change and three Na+ ions are pumped out of the cell across the plasma membrane and two K+ ions are pumped in the opposite direction into the cell. Both ions are being moved up their concentration gradients across the membrane; hence the requirement for an input of energy. No transport occurs unless ATP is hydrolyzed, and no ATP is hydrolyzed if there is no Na+ and K+ to transport (i.e. it is a coupled system).