Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase

Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase

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-...

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Bibliographic Details
Main 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
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2021
Subjects:
Science::Biological sciences
tRNA Methyltransferase
Antibacterial
Online Access:https://hdl.handle.net/10356/150609
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Institution: Nanyang Technological University
Language: English
Description
Summary: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.

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