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Sankaranarayanan R, et al.  (1999) The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell 97(3):371-81

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.

Status: Published

Type: Journal Article

PubMed ID: 10319817

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Sankaranarayanan R Dock-Bregeon AC Romby P Caillet J Springer M Rees B Ehresmann C Ehresmann B Moras D Papers in SGD Colleagues in SGD PubMed Google Scholar

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