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1qf6
From Proteopedia
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'''STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA''' | '''STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA''' | ||
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[[Category: Rees, B.]] | [[Category: Rees, B.]] | ||
[[Category: Sankaranarayanan, R.]] | [[Category: Sankaranarayanan, R.]] | ||
| - | [[Category: | + | [[Category: Aminoacylation]] |
| - | [[Category: | + | [[Category: Amp]] |
| - | [[Category: | + | [[Category: Mrna]] |
| - | [[Category: | + | [[Category: Protein/rna]] |
| - | [[Category: | + | [[Category: Threonyl-trna synthetase]] |
| - | [[Category: | + | [[Category: Translational regulation]] |
| - | [[Category: | + | [[Category: Zinc]] |
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Revision as of 03:11, 3 May 2008
STRUCTURE OF E. COLI THREONYL-TRNA SYNTHETASE COMPLEXED WITH ITS COGNATE TRNA
Overview
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.
About this Structure
1QF6 is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1QF6 with [Aminoacyl-tRNA Synthetases]. Full crystallographic information is available from OCA.
Reference
The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site., Sankaranarayanan R, Dock-Bregeon AC, Romby P, Caillet J, Springer M, Rees B, Ehresmann C, Ehresmann B, Moras D, Cell. 1999 Apr 30;97(3):371-81. PMID:10319817 Page seeded by OCA on Sat May 3 06:11:36 2008
