Methionyl-tRNA(fMet) formyltransferase is important in translation initiation in prokariotes since it is responsible for the formylation of the methionyl moiety esterified to the 3' end of tRNA. It transfers 10-formyltetrahydrofolate to the L-methionyl-tRNA(fMet) which results in production of tetrahydrofolate and N-formylmethionyl-tRNA(fMet). Inactivation of this gene in Escherichia coli severely impairs growth of bacteria. Crystal Structure of Methionyl-tRNA Formyltransferase from Yersinia pestis complexed with L-methionine was solved at 2.26A resolution. The enzyme is composed of two domains (N-terminal 1-204 and C-terminal 213-314 ) with a short linker 205- 212 between them. Residues from 41 to 46 are disordered in the structure. L –methionine is situated in the N-terminal part of the protein in a cavity and coordinated by Asn109, His111, Gly120 and Asp147.