Na+, K+-ATPase: relation of conformational transitions to function.
In its native environment, Na+, K+-ATPase of the plasma membrane is an oligomer consisting of two or more of each of two major subunits. Na+ and K+ move across the membrane through the channels that exist between the catalytic subunits of this oligomer. Two distinct ligand-induced conformational transitions (one due to the binding of K+ and ATP to the enzyme, and the other resulting from the phosphorylation of the enzyme in the presence of Na+ and ATP) cause changes in the geometries of the intersubunit channels, and provide the necessary energy-linked gating mechanisms for the transmembrane movements of ions against electrochemical gradients.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000378:metabolism; D003432:Cross-Linking Reagents / Q000494:pharmacology; D004734:Energy Metabolism; D007473:Ion Channels / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D008970:Molecular Weight; D010766:Phosphorylation; D011188:Potassium / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation / Q000187:drug effects; D012964:Sodium / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D003432:Cross-Linking Reagents; D007473:Ion Channels; D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D012964:Sodium; D000254:Sodium-Potassium-Exchanging ATPase; D011188:Potassium