Backbone resonance assignment for the full length tRNA-(N1G37) methyltransferase of Pseudomonas aeruginosa
| Autor: | Julien Lescar, Yee Hwa Wong, Hui Qi Ng, Jeffrey Hill, Ann Zhufang Koay, Peter C. Dedon, CongBao Kang, Wenhe Zhong, Qianhui Nah, Yan Li |
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| Přispěvatelé: | Massachusetts Institute of Technology. Department of Biological Engineering |
| Rok vydání: | 2019 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Methyltransferase biology Stereochemistry Dimer 030303 biophysics Translation (biology) Biochemistry TRNA binding Cofactor Amino acid 03 medical and health sciences chemistry.chemical_compound chemistry Structural Biology Transfer RNA biology.protein Protein secondary structure 030304 developmental biology |
| Zdroj: | Josephina Lee |
| ISSN: | 1874-270X 1874-2718 |
| Popis: | Bacterial tRNA (guanine37-N1)-methyltransferase (TrmD) plays important roles in translation, making it an important target for the development of new antibacterial compounds. TrmD comprises two domains with the N-terminal domain binding to the S-adenosyl-l-methionine (SAM) cofactor and the C-terminal domain critical for tRNA binding. Bacterial TrmD is functional as a dimer. Here we report the backbone NMR resonance assignments for the full length TrmD protein of Pseudomonas aeruginosa. Most resonances were assigned and the secondary structure for each amino acid was determined according to the assigned backbone resonances. The availability of the assignment will be valuable for exploring molecular interactions of TrmD with ligands, inhibitors and tRNA. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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