Li, Y., Zhong, W., Koay, A.Z. et al. Biomol NMR Assign (2019) 13: 327. https://doi.org/10.1007/s12104-019-09900-2
Bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) plays important roles in translation, making it an important target for the development of new antibacterial compounds. TrmD comprises two domains with the N-terminal domain binding to the S-adenosyl-L-methionine (SAM) cofactor and the C-terminal domain critical for tRNA binding. Bacterial TrmD is func-tional as a dimer. Here we report the backbone NMR resonance assignments for the full length TrmD protein of Pseudomonas aeruginosa. Most resonances were assigned and the secondary structure for each amino acid was determined according to the assigned backbone resonances. The availability of the assignment will be valuable for exploring molecular interactions of TrmD with ligands, inhibitors and tRNA.
This research / project is supported by the National Medical Research Council, Singapore - NMRC OF-IRG Grant
Grant Reference no. : NMRC/OFIRG/0051/2017
This research / project is supported by the Agency for Science, Technology and Research - JCO Grant
Grant Reference no. : 1431AFG102/1331A028