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

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.

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Authors and Affiliations

1. UPR 9002, Structure des Macromolécules Biologiques et Mécanismes de Reconnaissance, Laboratoire de Biologie Structurale, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15, rue René Descartes, 67084, Strasbourg, France
   Gilbert Eriani, Franck Martin, Laurent Ador & Jean Gangloff
2. UPR 9004, Laboratoire de Biologic Structurale, Institut de Biologie Moléculaire et Cellulaire du CNRS, 15, rue René Descartes, 67084, Strasbourg, France
   Jean Cavarelli, Bernard Rees, Jean -Claude Thierry & Dino Moras

Authors

1. Gilbert Eriani
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2. Jean Cavarelli
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3. Franck Martin
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4. Laurent Ador
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5. Bernard Rees
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6. Jean -Claude Thierry
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7. Jean Gangloff
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8. Dino Moras
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Additional information

Based on a presentation made at a workshop— “Aminoacyl-tRNA Synthetases and the Evolution of the Genetic Code”—held at Berkeley, CA, July 17–20, 1994

Correspondence to: G. Eriani

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Eriani, G., Cavarelli, J., Martin, F. et al. The class II aminoacyl-tRNA synthetases and their active site: Evolutionary conservation of an ATP binding site.J Mol Evol 40, 499–508 (1995). https://doi.org/10.1007/BF00166618

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• Revised: 18 July 1994
• Issue Date: May 1995
• DOI: https://doi.org/10.1007/BF00166618

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