Crystal structure of a non-discriminating glutamyl-tRNA synthetase.
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Authors
Schulze, Jörg OMasoumi, Ava
Nickel, Daniel
Jahn, Martina
Jahn, Dieter
Schubert, Wolf-Dieter
Heinz, Dirk W
Issue Date
2006-09-01
Metadata
Show full item recordAbstract
Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA(Gln) is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS). This enzyme thus charges both tRNA(Glu) and tRNA(Gln) with glutamate. Discriminating GluRS (D-GluRS), found in some bacteria and all eukaryotes, exclusively generates Glu-tRNA(Glu). Here we present the first crystal structure of a non-discriminating GluRS from Thermosynechococcus elongatus (ND-GluRS(Tel)) in complex with glutamate at a resolution of 2.45 A. Structurally, the enzyme shares the overall architecture of the discriminating GluRS from Thermus thermophilus (D-GluRS(Tth)). We confirm experimentally that GluRS(Tel) is non-discriminating and present kinetic parameters for synthesis of Glu-tRNA(Glu) and of Glu-tRNA(Gln). Anticodons of tRNA(Glu) (34C/UUC36) and tRNA(Gln) (34C/UUG36) differ only in base 36. The pyrimidine base of C36 is specifically recognized in D-GluRS(Tth) by the residue Arg358. In ND-GluRS(Tel) this arginine residue is replaced by glycine (Gly366) presumably allowing both cytosine and the bulkier purine base G36 of tRNA(Gln) to be tolerated. Most other ND-GluRS share this structural feature, leading to relaxed substrate specificity.Citation
Crystal structure of a non-discriminating glutamyl-tRNA synthetase. 2006, 361 (5):888-97 J. Mol. Biol.Affiliation
Division of Structural Biology, German Research Centre for Biotechnology (GBF), Mascheroder Weg 1, D-38124 Braunschweig, Germany.Journal
Journal of molecular biologyPubMed ID
16876193Type
ArticleLanguage
enISSN
0022-2836ae974a485f413a2113503eed53cd6c53
10.1016/j.jmb.2006.06.054
Scopus Count
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