Functional consequences of alterations to amino acids at the M5S5 boundary of the Ca(2+)-ATPase of sarcoplasmic reticulum. Mutation Tyr763-->Gly uncouples ATP hydrolysis from Ca2+ transport.

Abstract excerpt

The roles of the hydrophobic side chains of residues Phe760, Ile761, Tyr763, Leu764, and Ile765 located at the M5S5 boundary of the Ca(2+)-ATPase of sarcoplasmic reticulum were analyzed by site-directed mutagenesis. Substitution of Tyr763 with glycine resulted in a new phenotypic variant of the Ca(2+)-ATPase that catalyzed a high rate of Ca(2+)-activated ATP hydrolysis without net accumulation of Ca2+ in the...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Amino Acid Sequence
• Share to Biological Transport