Structural basis for anticodon recognition by methionyl-tRNA synthetase
Structural basis for anticodon recognition by methionyl-tRNA synthetase
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DOI:
10.1038/nsmb988
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发表时间:
2005-10-01
影响因子:
16.8
通讯作者:
Nureki, O
中科院分区:
文献类型:
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作者:
Nakanishi, K;Ogiso, Y;Nureki, O
In the 2.7-angstrom resolution crystal structure of methionyl-tRNA synthetase (MetRS) in complex with tRNA(Met) and a methionyladenylate 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).