| Literature DB >> 10319817 |
R Sankaranarayanan1, A C Dock-Bregeon, P Romby, J Caillet, M Springer, B Rees, C Ehresmann, B Ehresmann, D Moras.
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 A resolution of the complex between tRNA(Thr) 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.Entities:
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Year: 1999 PMID： 10319817 DOI： 10.1016/s0092-8674(00)80746-1
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582