Article
Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: comparison with functionally related proteins.
Journal of molecular biology - 6 Jul 2001
Foloppe N, Sagemark J, Nordstrand K, Berndt K D, Nilsson L
Abstract excerpt
The chemistry of active-site cysteine residues is central to the activity of thiol-disulfide oxidoreductases of the thioredoxin superfamily. In these reactions, a nucleophilic thiolate is required, but the associated pK(a) values differ vastly in the superfamily, from less than 4 in DsbA to greater than 7 in Trx. The factors that stabilize this thiolate are, however, not clearly established. The glutaredoxins...
Topics
- Bacterial Proteins
- Binding Sites
- Computer Simulation
- Cysteine
- Enzyme Stability
- Escherichia coli
- Glutaredoxins
- Histidine
- Humans
- Hydrogen Bonding
- Kinetics
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Mutation