Article
Alkaline proteinase inhibitor of Pseudomonas aeruginosa: a mutational and molecular dynamics study of the role of N-terminal residues in the inhibition of Pseudomonas alkaline proteinase.
The Journal of biological chemistry - 11 Jul 2003
Feltzer Rhona E, Trent John O, Gray Robert D
Abstract excerpt
Alkaline proteinase inhibitor of Pseudomonas aeruginosa is a 11.5-kDa, high affinity inhibitor of the serralysin class of zinc-dependent proteinases secreted by several Gram-negative bacteria. X-ray crystallography of the proteinase-inhibitor complex reveals that five N-terminal inhibitor residues occupy the extended substrate binding site of the enzyme and that the catalytic zinc is chelated by the alpha-amino...
Topics
- Amino Acids
- Catalytic Domain
- Circular Dichroism
- Crystallography, X-Ray
- Ions
- Kinetics
- Models, Molecular
- Mutation
- Plasmids
- Polymerase Chain Reaction
- Protease Inhibitors
