The aminoacyl-tRNA synthetase family: modules at work

Bioessays. 1993 Oct;15(10):675-87. doi: 10.1002/bies.950151007.


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.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Amino Acid Sequence
  • Amino Acyl-tRNA Synthetases / chemistry*
  • Amino Acyl-tRNA Synthetases / classification
  • Amino Acyl-tRNA Synthetases / metabolism
  • Catalysis
  • Consensus Sequence
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation*
  • Protein Folding
  • Protein Structure, Tertiary
  • RNA, Transfer / metabolism
  • RNA, Transfer, Amino Acyl / biosynthesis
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship


  • RNA, Transfer, Amino Acyl
  • RNA, Transfer
  • Amino Acyl-tRNA Synthetases