Structural and functional relationships between aminoacyl-tRNA synthetases
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Updated: Oct 16, 2026

Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
Published on: February 25, 2011
1Institut de Biologie, Moléculaire et Cellulaire du CNRS, Laboratoire de Cristallographie Biologique, Strasbourg, France.
Abstract:
Aminoacyl-tRNA synthetases can be divided in two groups of equal size on the basis of differences in the structure of their active sites. The core of class I synthetases is the classical nucleotide-binding domain with its characteristic Rossmann fold. In contrast, the active site of class II synthetases is built around an antiparallel beta-sheet, to which the substrates bind. This classification, which is based on structural data (amino acid sequences and tertiary structures), can be rationalized in functional terms.
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