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Nucleic Acids Symp Ser. 1995;(33):40-2.

Substrate selection by aminoacyl-tRNA synthetases.

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1
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511, USA.

Abstract

The integration of genetic and biochemical approaches to study the crystal structure of the glutaminyl-tRNA synthetase (GlnRS):tRNA(Gln):ATP complex has elucidated the mechanism by which GlnRS selects its cognate tRNA for aminoacylation. Three principal types of interaction have been identified: interaction with specific bases in the cognate tRNA, rejection of non-cognate tRNAs, and activation of the active site upon cognate tRNA binding. The recent solving of the crystal structure of tryptophanyl-tRNA synthetase (TrpRS) has allowed comparable studies to be initiated in an aminoacyl-tRNA synthetase which, unlike GlnRS, does not require tRNA binding prior to amino acid activation.

PMID:
8643392
[Indexed for MEDLINE]
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