earticle

영어

Amino acyl tRNA synthetase (AARS) is an ATP dependent enzyme helps in charging of tRNA with cognate amino acid during protein synthesis. The accuracy of the protein translation is maintained by the proof reading activity of AARS by preventing charging of tRNA with non cognate amino acids (Unnatural amino acids). Recently researchers identified a methodology in which the endogenous tRNA synthetases can recognize and incorporate the close structural analogs of the cognate amino acid containing novel functional groups in the absence of the natural substrate called as codon reassignment. Currently, more than 15 methionine analogs were incorporated into protein in response to the sense codon with the help of methionine auxotrophic cell which provide novel application such as metabolic labeling. In this study, we have performed molecular docking analysis to predict the binding mode of the methionine analogs with the active site residues of Escherichia coli methionyl tRNA synthetase and we identified the key residues responsible for the recognition of these methionine analogs. Here, we clearly demonstrate the substrate selectivity of these methionine analogs with methionyl tRNA synthetase and offer the clear structural knowledge about the active site which will provide knowledge for rational designing of methionyl tRNA synthetase.