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The aminoacyl‐tRNA synthetase family: Modules at work
Author(s) -
Delarue M.,
Moras D.
Publication year - 1993
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.950151007
Subject(s) - aminoacyl trna synthetase , transfer rna , folding (dsp implementation) , function (biology) , computational biology , sequence (biology) , nucleotide , biology , amino acid , biochemistry , genetics , rna , gene , electrical engineering , engineering
The combined use of molecular and structural biology techniques has proved very efficient in elucidating structure‐function relationships in aminoacyl‐tRNA synthetases. Our present understanding of this family of enzymes is based on two main unifying principles: (i) division into two different classes, corresponding to two different modes of ATP binding and attachment of the activated amino acid to the last nucleotide of tRNA (either 2′OH or 3′OH of the ribose) by two different catalytic mechanisms and two structural domains with completely different folding, and (ii) the modular organization into separate and additional domains that we are just beginning to understand. Sequence analysis complements very nicely existing structural, biochemical and genetic results and makes them more general, leading to verifiable predictions.