Backbone resonance assignment for the full length tRNA-(N1G37) methyltransferase of Pseudomonas aeruginosa

Backbone resonance assignment for the full length tRNA-(N1G37) methyltransferase of Pseudomonas aeruginosa

Biomolecular NMR Assignments

10.1007/s12104-019-09900-2

https://doi.org/10.1007/s12104-019-09900-2

Yan Li, Wenhe Zhong, Ann Zhufang Koay, Hui Qi Ng, Qianhui Nah, Yee Hwa Wong, Jeffrey Hill, Julien Lescar, Peter C. Dedon, Congbao Kang

TrmD, Pseudomonas aeruginosa, tRNA methyltransferase, Epitranscriptome, drug discovery, Antibacterial, protein dynamics, Backbone assignment

07 June 2019

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.

PublisherCopyrights

NMRC OF-IRG Grant (NMRC/OFIRG/0051/2017) and A*STAR JCO Grant (1431AFG102/1331A028).

https://astaroar.ripplewerkz.co/communities-collections/articles/14407

1874-2718

Experimental Drug Development Centre