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    Crystal structure of a non-discriminating glutamyl-tRNA synthetase.

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    Authors
    Schulze, Jörg O
    Masoumi, Ava
    Nickel, Daniel
    Jahn, Martina
    Jahn, Dieter
    Schubert, Wolf-Dieter
    Heinz, Dirk W
    Issue Date
    2006-09-01
    
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    Abstract
    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 biology
    URI
    http://hdl.handle.net/10033/15230
    DOI
    10.1016/j.jmb.2006.06.054
    PubMed ID
    16876193
    Type
    Article
    Language
    en
    ISSN
    0022-2836
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.jmb.2006.06.054
    Scopus Count
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