Article
Structure and function of a serine carboxypeptidase adapted for degradation of the protein synthesis antibiotic microcin C7.
Proceedings of the National Academy of Sciences of the United States of America - 20 Mar 2012
Agarwal Vinayak, Tikhonov Anton, Metlitskaya Anastasia, Severinov Konstantin, Nair Satish K
Abstract excerpt
Several classes of naturally occurring antimicrobials exert their antibiotic activity by specifically targeting aminoacyl-tRNA synthetases, validating these enzymes as drug targets. The aspartyl tRNA synthetase "Trojan horse" inhibitor microcin C7 (McC7) consists of a nonhydrolyzable aspartyl-adenylate conjugated to a hexapeptide carrier that facilitates active import into bacterial cells through an oligopeptide...
Topics
- Amides
- Amino Acyl-tRNA Synthetases
- Bacteria
- Bacteriocins
- Carboxypeptidases
- Catalysis
- Catalytic Domain
- Crystallography, X-Ray
- Hydrolysis
- Kinetics
- Models, Molecular
- Molecular Conformation
- Mutation