Article
Mutational analysis of the conserved TGES loop of sarcoplasmic reticulum Ca2+-ATPase.
The Journal of biological chemistry - 20 Oct 2006
Anthonisen Anne Nyholm, Clausen Johannes D, Andersen Jens Peter
Abstract excerpt
Crystal structures have shown that the conserved TGES loop of the Ca2+-ATPase is isolated in the Ca2E1 state but becomes inserted in the catalytic site in E2 states. Here, we have examined the kinetics of the partial reaction steps of the transport cycle and the binding of the phosphoryl analogs BeF, AlF, MgF, and vanadate in mutants with alterations to the TGES residues. The mutations encompassed variation of...
Topics
- Aluminum Compounds
- Animals
- Biological Transport
- Catalytic Domain
- DNA Mutational Analysis
- Fluorides
- Hydrogen Bonding
- Models, Chemical
- Models, Molecular
- Mutation
- Phosphorylation
- Protein Binding
- Protein Structure, Tertiary
- Rabbits
- Sarcoplasmic Reticulum Calcium-Transporting ATPases
- Vanadates