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- W2114972602 abstract "E. coli threonyl-tRNA synthetase (ThrRS) is a class II enzyme that represses the translation of its own mRNA. We report the crystal structure at 2.9 Å resolution of the complex between tRNAThr and ThrRS, whose structural features reveal novel strategies for providing specificity in tRNA selection. These include an amino-terminal domain containing a novel protein fold that makes minor groove contacts with the tRNA acceptor stem. The enzyme induces a large deformation of the anticodon loop, resulting in an interaction between two adjacent anticodon bases, which accounts for their prominent role in tRNA identity and translational regulation. A zinc ion found in the active site is implicated in amino acid recognition/discrimination." @default.
- W2114972602 created "2016-06-24" @default.
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- W2114972602 date "1999-04-01" @default.
- W2114972602 modified "2023-10-18" @default.
- W2114972602 title "The Structure of Threonyl-tRNA Synthetase-tRNAThr Complex Enlightens Its Repressor Activity and Reveals an Essential Zinc Ion in the Active Site" @default.
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- W2114972602 doi "https://doi.org/10.1016/s0092-8674(00)80746-1" @default.
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