Crystal structure and catalytic mechanism of the essential m¹G37 tRNA methyltransferase TrmD from Pseudomonas aeruginosa

• Main Authors: Juthamas Jaroensuk, Yee Hwa Wong, Wenhe Zhong, Chong Wai Liew, Somchart Maenpuen, Abbas E. Sahili, Sopapan Atichartpongkul, Yok Hian Chionh, Qianhui Nah, Narumon Thongdee, Megan E. McBee, Erin G. Prestwich, Michael S. Demott, Pimchai Chaiyen, Skorn Mongkolsuk, Peter C. Dedon, Julien Lescar, Mayuree Fuangthong
• Other Authors: Singapore-MIT Alliance for Research and Technology
• Format: Article
• Published: 2020
• Subjects: Biochemistry, Genetics and Molecular Biology
• Online Access: https://repository.li.mahidol.ac.th/handle/123456789/50407
• Institution: Mahidol University

© 2019 Cold Spring Harbor Laboratory Press. All rights reserved. The tRNA (m1G37) methyltransferase TrmD catalyzes m1G formation at position 37 in many tRNA isoacceptors and is essential in most bacteria, which positions it as a target for antibiotic development. In spite of its crucial role, little...