Article
Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.
The Journal of biological chemistry - 29 Apr 1994
Flaherty K M, Wilbanks S M, DeLuca-Flaherty C, McKay D B
Abstract excerpt
The ATPase fragment of the bovine 70-kDa heat shock cognate protein is an attractive construct in which to study its mechanism of ATP hydrolysis. The three-dimensional structure suggests several residues that might participate in the ATPase reaction. Four acidic residues (Asp-10, Glu-175, Asp-199...
Topics
- Adenosine Diphosphate
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Animals
- Binding Sites
- Carrier Proteins
- Cattle
- Computer Graphics
- HSC70 Heat-Shock Proteins
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- Hydrolysis
- Kinetics
- Models, Molecular
- Mutation
- Protein Conformation
- Structure-Activity Relationship