Structural basis for the E1/E1P-E2/E2P conformation changes in the sarcoplasmic reticulum Ca(2+)-ATPase studied by site-specific mutagenesis.
Site-specific mutagenesis and functional expression of cloned cDNA of the sarcoplasmic reticulum Ca(2+)-ATPase have been used to demonstrate that exchange of single amino acid residues in the Ca(2+)-ATPase can lead to forms with either "E1/E1P" or "E2/E2P" characteristics. The localization of the mutated residues identifies the M4S4 segment of the ATPase molecule as central to the energy-tranducing conformation change, and on the basis of this information a model for the pump mechanism is discussed.
Andersen
J P
JP
Danish Biomembrane Research Centre, University of Aarhus.
Vilsen
B
B
D000818:Animals; D000252:Calcium-Transporting ATPases / Q000235:genetics / Q000378:metabolism*; D004247:DNA / Q000378:metabolism; D008956:Models, Chemical; D009132:Muscles / Q000201:enzymology / Q000648:ultrastructure; D016296:Mutagenesis; D010766:Phosphorylation; D011487:Protein Conformation; D011817:Rabbits; D012519:Sarcoplasmic Reticulum / Q000201:enzymology*
D004247:DNA; D000252:Calcium-Transporting ATPases