Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase
Author(s)
Li, Yan
Zhong, Wenhe
Koay, Ann Zhufang
Ng, Hui Qi
Koh-Stenta, Xiaoying
Nah, Qianhui
Lim, Siau Hoi
Larsson, Andreas
Lescar, Julien
Hill, Jeffrey
Date Issued
October 2018
Journal
Biomolecular NMR Assignments
Publisher
Springer Science and Business Media LLC
Citation
Li, Y. et al. Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase. Biomolecular NMR Assignments 13 (April 2019): 49–53 © 2018 Springer Nature
Version
Author's final manuscript
Abstract
Bacterial tRNA (guanine³⁷-N¹)-methyltransferase (TrmD) is an important antibacterial target due to its essential role in translation. TrmD has two domains connected with a flexible linker. The N-terminal domain (NTD) of TrmD contains the S-adenosyl-l-methionine (SAM) cofactor binding site and the C-terminal domain is critical for tRNA binding. Here we report the backbone NMR resonance assignments for NTD of Pseudomonas aeruginosa TrmD. Its secondary structure was determined based on the assigned resonances. Relaxation analysis revealed that NTD existed as dimers in solution. NTD also exhibited thermal stability in solution. Its interactions with SAM and other compounds suggest it can be used for evaluating SAM competitive inhibitors by NMR.
MIT Department
Singapore-MIT Alliance in Research and Technology (SMART)
Massachusetts Institute of Technology. Department of Biological Engineering
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1007/s12104-018-9849-9
