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-...
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: | Journal Article |
Language: | English |
Published: |
2021
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/150609 |
Similar Items
-
Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase
by: Li, Yan, et al.
Published: (2020) -
Targeting the bacterial epitranscriptome for antibiotic development : discovery of novel tRNA-(N1G37) methyltransferase (TrmD) inhibitors
by: Zhong, Wenhe, et al.
Published: (2021) -
Backbone resonance assignment for the full length tRNA-(N1G37) methyltransferase of Pseudomonas aeruginosa
by: Li, Yan, et al.
Published: (2020) -
Required Elements in tRNA for Methylation by the Eukaryotic tRNA (Guanine-<i>N</i><sup>2</sup>-) Methyltransferase (Trm11-Trm112 Complex)
by: Yu Nishida, et al.
Published: (2022-04-01) -
Thienopyrimidinone derivatives that inhibit bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) by restructuring the active site with a tyrosine-flipping mechanism
by: Zhong, Wenhe, et al.
Published: (2021)