Article
Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase.
The EMBO journal - 1 Aug 1997
Schmitt E, Mechulam Y, Fromant M, Plateau P, Blanquet S
Abstract excerpt
Peptidyl-tRNA hydrolase activity from Escherichia coli ensures the recycling of peptidyl-tRNAs produced through abortion of translation. This activity, which is essential for cell viability, is carried out by a monomeric protein of 193 residues. The structure of crystalline peptidyl-tRNA hydrolas...
Topics
- Aeromonas
- Amino Acid Sequence
- Binding Sites
- Carboxylic Ester Hydrolases
- Crystallography, X-Ray
- Escherichia coli
- Genes, Bacterial
- Models, Molecular
- Molecular Sequence Data
- Molecular Structure
- Mutagenesis, Site-Directed
- Mutation
- Protein Conformation
- Protein Structure, Secondary
- Sequence Homology, Amino Acid
- Species Specificity
- Substrate Specificity