Article
Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli.
The Journal of biological chemistry - 7 Apr 1995
Seol J H, Baek S H, Kang M S, Ha D B, Chung C H
Abstract excerpt
ClpA is the ATPase component of the ATP-dependent protease Ti (Clp) in Escherichia coli and contains two ATP-binding sites. A ClpA variant (referred to as ClpAT) carrying threonine in place of the 169th methionine has recently been shown to be highly soluble but indistinguishable from the wild-ty...
Topics
- Adenosine Triphosphatases
- Adenosine Triphosphate
- Base Sequence
- Binding Sites
- Biopolymers
- DNA Primers
- Endopeptidase Clp
- Escherichia coli
- Escherichia coli Proteins
- Hydrolysis
- Molecular Sequence Data
- Mutation
- Serine Endopeptidases