Exploring the Crystal Structure of tRNA Methyltransferase from Mycobacterium abscessus

Here we investigate the catalytic site of tRNA methyltransferase enzyme (TrmD) in Mycobacterium abscessus as a potential antibiotic target. Previously, molecular dynamic simulation has been employed to predict the relationship between the natural ligand, S-adenosyl-L-methionine, and a divalent metallic ion. However no experimental crystallographic evidence has been obtained thus far. Three protein structures of this TrmD with S-adenosyl-L-homocysteine have been determined by X-ray crystallography. Here we report the first structure to be found with the cationic magnesium bound in the catalytic site. The models and analysis provided in this study offer insight into the complex methylation reaction that occurs in the catalytic site and overall means of survival for certain infectious bacteria. This work directly contributes to pharmaceutical efforts in creating antimicrobial treatments with TrmD acting as a potential drug target.