Structural basis for anticodon recognition by methionyl-tRNA synthetase.
Nakanishi, K., Ogiso, Y., Nakama, T., Fukai, S., Nureki, O.(2005) Nat Struct Mol Biol 12: 931-932
- PubMed: 16155581 
- DOI: https://doi.org/10.1038/nsmb988
- Primary Citation of Related Structures:  
2CSX, 2CT8 - PubMed Abstract: 
In the 2.7-A resolution crystal structure of methionyl-tRNA synthetase (MetRS) in complex with tRNA(Met) and a methionyl-adenylate analog, the tRNA anticodon loop is distorted to form a triple-base stack comprising C34, A35 and A38. A tryptophan residue stacks on C34 to extend the triple-base stack. In addition, C34 forms Watson-Crick-type hydrogen bonds with Arg357. This structure resolves the longstanding question of how MetRS specifically recognizes tRNA(Met).
Organizational Affiliation: 
Department of Biological Information, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, Yokohama-shi, Kanagawa 226-8501, Japan.