Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase.
Article Details
- CitationCopy to clipboard
Fourmy D, Mechulam Y, Brunie S, Blanquet S, Fayat G
Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase.
FEBS Lett. 1991 Nov 4;292(1-2):259-63.
- PubMed ID
- 1959615 [ View in PubMed]
- Abstract
Comparison of the amino-acid sequences of several methionyl-tRNA synthetases indicates the occurrence of a few conserved motifs, having a possible functional significance. The role of one of these motifs, centered at position 300 in the E. coli enzyme sequence, was assayed by the use of site-directed mutagenesis. Substitution of the His301 or Trp305 residues by Ala resulted in a large decrease in methionine affinity, whereas the change of Val298 into Ala had only a moderate effect. The catalytic rate of the enzyme was unimpaired by these substitutions. It is concluded that the above conserved amino-acid region is located at or close to the amino-acid binding pocket of methionyl-tRNA synthetase.