Structural basis for anticodon recognition by methionyl-tRNA synthetase.
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).
Nakanishi
Kotaro
K
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.
Ogiso
Yuri
Y
Nakama
Takashi
T
Fukai
Shuya
S
Nureki
Osamu
O
D000595:Amino Acid Sequence; D000926:Anticodon / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology* / Q000235:genetics; D003461:Crystallography; D008718:Methionine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012358:RNA, Transfer, Met / Q000737:chemistry*
D000926:Anticodon; D012358:RNA, Transfer, Met; D008718:Methionine-tRNA Ligase