期刊
NATURE STRUCTURAL BIOLOGY
卷 8, 期 3, 页码 203-206出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/84927
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Glutamyl-tRNA synthetases (GluRSs) are divided into two distinct types, with regard to the presence or absence of glutaminyl-tRNA synthetase (GlnRS) in the genetic translation systems. In the original 19-synthetase systems lacking GlnRS, the 'non-discriminating' GluRS glutamylates both tRNA(Glu) and tRNA(Gln) In contrast, in the evolved 20-synthetase systems with GlnRS, the 'discriminating' GluRS aminoacylates only tRNA(Glu). Here we report the 2.4 Angstrom resolution crystal structure of a 'discriminating' GluRS.tRNA(Glu) complex from Thermus thermophilus. The GluRS recognizes the tRNA(Glu) anticodon bases via two a-helical domains, maintaining the base stacking. We show that the discrimination between the Glu and Gin anticodons ((YUC36)-Y-34 and (34)YUG(36), respectively) is achieved by a single arginine residue (Arg 358). The mutation of Arg 358 to Gin resulted in a GluRS that does not discriminate between the Glu and Gin anticodons. This change mimics the reverse course of GluRS evolution from anticodon 'non-dicsriminating' to 'discriminating'.
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