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Identification of the nucleophilic factors and the productive complex for the editing reaction by leucyl‐tRNA synthetase
Author(s) -
Hagiwara Yohsuke,
Nureki Osamu,
Tateno Masaru
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.05.026
Subject(s) - nucleophile , transfer rna , translation (biology) , amino acyl trna synthetases , aminoacyl trna synthetase , chemistry , identification (biology) , aminoacyl trna , stereochemistry , biology , biochemistry , rna , messenger rna , catalysis , gene , ecology
To ensure fidelity of translation, several aminoacyl‐tRNA synthetases (aaRSs) possess editing capability to hydrolyse mis‐aminoacylated tRNAs. In this report, based on our previously‐modelled structure of leucyl‐tRNA synthetase (LeuRS) complexed with valyl‐tRNA Leu , further structural modelling has been performed along with molecular dynamics simulations. This enabled the identification of the nucleophile, which is different from that suggested by the crystal structure of the LeuRS • Nva2AA complex. Our results revealed that the 3′ hydroxyl group of A76 acts as a “gate” to regulate the accessibility of the nucleophile; thus, the opening of the gate leads to the productive complex for the reaction.