1QF6

STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA

Summary for 1QF6

• Entry DOI: 10.2210/pdb1qf6/pdb
• Descriptor: THREONINE TRNA, THREONYL-TRNA SYNTHETASE, ZINC ION, ... (5 entities in total)
• Functional Keywords: threonyl-trna synthetase, trna(thr), amp, mrna, aminoacylation, translational regulation, protein/rna, ligase-rna complex, ligase/rna
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P0A8M3
• Total number of polymer chains: 2
• Total formula weight: 99167.72

Authors

Sankaranarayanan, R.,Dock-Bregeon, A.C.,Rees, B.,Moras, D. (deposition date: 1999-04-06, release date: 1999-05-06, Last modification date: 2023-12-27)

Primary citation

Sankaranarayanan, R.,Dock-Bregeon, A.C.,Romby, P.,Caillet, J.,Springer, M.,Rees, B.,Ehresmann, C.,Ehresmann, B.,Moras, D.
The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site
Cell(Cambridge,Mass.), 97:371-381, 1999

PubMed 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.

PubMed: 10319817
DOI: 10.1016/S0092-8674(00)80746-1

Experimental method

X-RAY DIFFRACTION (2.9 Å)