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Trends Biochem Sci. 1992 Apr;17(4):159-64.

Structural and functional relationships between aminoacyl-tRNA synthetases.

Author information

1
Institut de Biologie, Mol├ęculaire 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.

PMID:
1585461
[Indexed for MEDLINE]

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