Article
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.
The Journal of biological chemistry - 13 Jan 1995
Andersen J P
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 C...
Topics
- Adenosine Triphosphate
- Amino Acid Sequence
- Animals
- Biological Transport
- Calcium
- Calcium-Transporting ATPases
- Glycine
- Hydrolysis
- Molecular Sequence Data
- Mutation
- Phosphates
- Phosphorylation
- Protein Conformation
- Rabbits
- Sarcoplasmic Reticulum
- Tyrosine