Structural basis for anticodon recognition by methionyl-tRNA synthetase

Kotaro Nakanishi; Yuri Ogiso; Takashi Nakama; Shuya Fukai; Osamu Nureki

doi:10.1038/nsmb988

Structural basis for anticodon recognition by methionyl-tRNA synthetase

Nat Struct Mol Biol. 2005 Oct;12(10):931-2. doi: 10.1038/nsmb988. Epub 2005 Sep 11.

Authors

Kotaro Nakanishi¹, Yuri Ogiso, Takashi Nakama, Shuya Fukai, Osamu Nureki

Affiliation

¹ 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.

PMID: 16155581
DOI: 10.1038/nsmb988

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).

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Anticodon / metabolism*
Bacteria / enzymology*
Bacteria / genetics
Crystallography
Methionine-tRNA Ligase / chemistry*
Methionine-tRNA Ligase / metabolism*
Molecular Sequence Data
Nucleic Acid Conformation
Protein Conformation
RNA, Transfer, Met / chemistry*

Substances

Anticodon
RNA, Transfer, Met
Methionine-tRNA Ligase

Associated data

PDB/2CSX
PDB/2CT8