Article
Amino acid binding by the class I aminoacyl-tRNA synthetases: role for a conserved proline in the signature sequence.
Protein science : a publication of the Protein Society - 1 May 1992
Burbaum J J, Schimmel P
Abstract excerpt
Although partial or complete three-dimensional structures are known for three Class I aminoacyl-tRNA synthetases, the amino acid-binding sites in these proteins remain poorly characterized. To explore the methionine binding site of Escherichia coli methionyl-tRNA synthetase, we chose to study a specific, randomly generated methionine auxotroph that contains a mutant methionyl-tRNA synthetase whose defect is...
Topics
- Amino Acid Sequence
- Cloning, Molecular
- Consensus Sequence
- Escherichia coli
- Kinetics
- Methionine
- Methionine-tRNA Ligase
- Models, Molecular
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Phenotype