Article
A site in the dinucleotide-fold domain contributes to the accuracy of tRNA selection by Escherichia coli methionyl-tRNA synthetase.
Molecules and cells - 31 Oct 1998
Kim H Y, Pak M, Jakubowski H
Abstract excerpt
Interactions of specific amino acid residues of the carboxyl-terminal domain of MetRS with the CAU anticodon of tRNAMet assure accurate and efficient aminoacylation. The substitution of one such residue, Trp461 by Phe, impairs the binding of cognate tRNA, but enhances the binding of noncognate tR...
Topics
- Anticodon
- Binding Sites
- Escherichia coli
- Genetic Variation
- Methionine-tRNA Ligase
- Nucleic Acid Conformation
- Oligonucleotides
- RNA, Transfer, Amino Acyl
- RNA, Transfer, Met