The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Cell Année : 1999

The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site

Résumé

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.

Dates et versions

hal-04014359 , version 1 (03-03-2023)

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Citer

R. Sankaranarayanan, Anne-Catherine Dock Bregeon, Pascale Romby, Joel Caillet, M. Springer, et al.. The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site. Cell, 1999, 97 (3), pp.371-381. ⟨10.1016/s0092-8674(00)80746-1⟩. ⟨hal-04014359⟩
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