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: | , , , , , , , , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2021
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| Subjects: | |
| Online Access: | https://hdl.handle.net/10356/150609 |
| _version_ | 1826116061381001216 |
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| author | 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 |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences 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 |
| author_sort | Yan, Li |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T04:05:15Z |
| format | Journal Article |
| id | ntu-10356/150609 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T04:05:15Z |
| publishDate | 2021 |
| record_format | dspace |
| spelling | ntu-10356/1506092021-06-07T07:20:21Z Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase 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 School of Biological Sciences Institute of Structural Biology Science::Biological sciences tRNA Methyltransferase Antibacterial 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. Agency for Science, Technology and Research (A*STAR) National Research Foundation (NRF) Singapore-MIT Alliance for Research and Technology (SMART) CK appreciates the support from A*STAR JCO grant (1431AFG102/1331A028). This work is also supported by National Research Foundation of Singapore through the Singapore-MIT-Alliance for Research and Technology (SMART) Infectious Disease and Antimicrobial Resistance Interdisciplinary Research Groups. W.Z. was supported by a SMART Scholar Fellowship. We also thank Prof Ho Sup Yoon and Dr. Hong Ye from Nanyang Technological University for the supporting NMR experiments. The authors appreciate the valuable discussion from the team members at ETC, A*STAR. 2021-06-07T07:20:21Z 2021-06-07T07:20:21Z 2019 Journal Article 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 1874-2718 0000-0002-9886-9374 https://hdl.handle.net/10356/150609 10.1007/s12104-018-9849-9 30298375 2-s2.0-85055053725 1 13 49 53 en 1431AFG102 1331A028 Biomolecular NMR Assignments © 2018 Springer Nature B. V. All rights reserved. |
| spellingShingle | Science::Biological sciences tRNA Methyltransferase Antibacterial 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 Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase |
| title | Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase |
| title_full | Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase |
| title_fullStr | Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase |
| title_full_unstemmed | Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase |
| title_short | Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N1G37) methyltransferase |
| title_sort | backbone resonance assignment for the n terminal region of bacterial trna n1g37 methyltransferase |
| topic | Science::Biological sciences tRNA Methyltransferase Antibacterial |
| url | https://hdl.handle.net/10356/150609 |
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