Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/150609
Title: Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase
Authors: Yan, Li 
Zhong, Wenhe
Koay, Ann Zhufang
Ng, Hui Qi
Koh‑Stenta, Xiaoying
Nah, Qianhui
Lim, Siau Hoi
Larsson, Andreas
Lescar, Julien
Hill, Jeffrey
Dedon, Peter C.
Kang, CongBao
Keywords: Science::Biological sciences
Issue Date: 2019
Source: Yan, L., Zhong, W., Koay, A. Z., Ng, H. Q., Koh‑Stenta, X., Nah, Q., Lim, S. H., Larsson, A., Lescar, J., Hill, J., Dedon, P. C. & Kang, C. (2019). Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase. Biomolecular NMR Assignments, 13(1), 49-53. https://dx.doi.org/10.1007/s12104-018-9849-9
Project: 1431AFG102
1331A028
Journal: Biomolecular NMR Assignments
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.
URI: https://hdl.handle.net/10356/150609
ISSN: 1874-2718
DOI: 10.1007/s12104-018-9849-9
Rights: © 2018 Springer Nature B. V. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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