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Related Experiment Videos

Structural basis for tRNA-dependent amidotransferase function.

Emmanuelle Schmitt1, Michel Panvert, Sylvain Blanquet

  • 1Laboratoire de Biochimie, Unité Mixte de Recherche 7654, CNRS-Ecole Polytechnique, F-91128 Palaiseau cedex, France. emma@botrytis.polytechnique.fr

Structure (London, England : 1993)
|October 12, 2005
PubMed
Summary

This study reveals the structure of a tRNA-dependent amidotransferase, GatDE, essential for protein synthesis. The findings illuminate the mechanism of amino acid attachment to tRNA via indirect routes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Aminoacyl-tRNA synthetases directly charge tRNAs with amino acids.
  • Indirect amino acid attachment routes to tRNA exist, potentially explaining the evolution of protein synthesis.
  • In archaea and bacteria, glutamine is attached to tRNA(Gln) via a two-step process involving misacylation and a tRNA-dependent amidotransferase.

Purpose of the Study:

  • To determine the structure of the tRNA-dependent amidotransferase GatDE from Pyrococcus abyssi.
  • To elucidate the mechanism of tRNA-dependent amino acid amination.

Main Methods:

  • X-ray crystallography at 3.0 Å resolution.
  • Structural analysis of the GatDE tetramer.
  • Comparison with L-asparaginase structures.

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Main Results:

  • The crystal structure of GatDE reveals a tetrameric complex with GatD core and GatE peripheral subunits.
  • The fold of GatE is distinct from known tRNA-binding enzymes.
  • The ammonium donor site on GatD and the tRNA binding site on GatE are spatially separated.
  • A mobile beta hairpin in GatD, containing a catalytic threonine, is proposed to regulate the reaction cycle.

Conclusions:

  • The structure of GatDE provides insights into the mechanism of indirect amino acid attachment to tRNA.
  • The distinct domain organization and catalytic mechanism highlight the unique nature of tRNA-dependent amidotransferases.
  • Understanding GatDE function contributes to knowledge of protein synthesis evolution and regulation.