Backbone resonance assignment for the full length tRNA-(N1G37) methyltransferase of Pseudomonas aeruginosa
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 functional 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.
KeywordsTrmD Pseudomonas aeruginosa tRNA methyltransferase Epitranscriptome Drug discovery Antibacterial Protein dynamics Backbone assignment
CK appreciates the support from NMRC OF-IRG Grant (NMRC/OFIRG/0051/2017) and A*STAR JCO Grant (1431AFG102/1331A028). This work is also supported by National Research Foundation of Singapore through the Singapore-MIT-Alliance for Research and Technology (SMART) Infectious Disease and Antimicrobial Resistance Interdisciplinary Research Groups. WZ was supported by a SMART Scholar Fellowship. We also thank Prof Ho Sup Yoon and Dr. Hong Ye from Nanyang Technological University for the NMR experiments. The authors appreciate the valuable discussion from the team members at EDDC, A*STAR.
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Conflict of interest
The authors declare that they have no conflict of interest.
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