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Journal of Molecular Evolution

, Volume 40, Issue 5, pp 499–508 | Cite as

The class II aminoacyl-tRNA synthetases and their active site: Evolutionary conservation of an ATP binding site

  • Gilbert Eriani
  • Jean Cavarelli
  • Franck Martin
  • Laurent Ador
  • Bernard Rees
  • Jean -Claude Thierry
  • Jean Gangloff
  • Dino Moras
Articles

Abstract

Previous sequence analyses have suggested the existence of two distinct classes of aminoacyl-tRNA synthetase. The partition was established on the basis of exclusive sets of sequence motifs (Eriani et al. [1990] Nature 347:203–306). X-ray studies have now well defined the structural basis of the two classes: the class I enzymes share with dehydrogenases and kinases the classic nucleotide binding fold called the Rossmann fold, whereas the class II enzymes possess a different fold, not found elsewhere, built around a six-stranded antiparallel β-sheet. The two classes of synthetases catalyze the same global reaction that is the attachment of an amino acid to the tRNA, but differ as to where on the terminal adenosine of the tRNA the amino acid is placed: class I enzymes act on the 2′ hydroxyl whereas the class II enzymes prefer the 3′ hydroxyl group. The three-dimensional structure of aspartyl-tRNA synthetase from yeast, a typical class II enzyme, is described here, in relation to its function. The crucial role of the sequence motifs in substrate binding and enzyme structure is high-lighted. Overall these results underline the existence of an intimate evolutionary link between the aminoacyl-tRNA synthetases, despite their actual structural diversity.

Key words

Two classes of aminoacyl-tRNA synthetases Sequence comparisons Homology X-ray structure Structure-function relationships Origin of aminoacyl-tRNA synthetases Two ancestral molecules Genetic code 
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Copyright information

© Springer-Verlag New York Inc 1995

Authors and Affiliations

  • Gilbert Eriani
    • 1
  • Jean Cavarelli
    • 2
  • Franck Martin
    • 1
  • Laurent Ador
    • 1
  • Bernard Rees
    • 2
  • Jean -Claude Thierry
    • 2
  • Jean Gangloff
    • 1
  • Dino Moras
    • 2
  1. 1.UPR 9002, Structure des Macromolécules Biologiques et Mécanismes de ReconnaissanceLaboratoire de Biologie Structurale, Institut de Biologie Moléculaire et Cellulaire du CNRSStrasbourgFrance
  2. 2.UPR 9004, Laboratoire de Biologic StructuraleInstitut de Biologie Moléculaire et Cellulaire du CNRSStrasbourgFrance

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