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Related Experiment Videos

How glutaminyl-tRNA synthetase selects glutamine

V L Rath1, L F Silvian, B Beijer

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, PO Box 208114, New Haven, CT 06520-8114, USA.

Structure (London, England : 1993)
|May 20, 1998
PubMed
Summary

Glutaminyl-tRNA synthetase (GlnRS) uses specific interactions to select glutamine over glutamic acid. The crystal structure reveals how tRNA binding influences amino acid activation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Aminoacyl-tRNA synthetases (aaRS) are crucial enzymes ensuring protein synthesis fidelity.
  • Glutaminyl-tRNA synthetase (GlnRS) exhibits a unique mechanism requiring tRNA binding prior to amino acid activation.
  • Understanding GlnRS substrate specificity necessitates structural analysis of the enzyme with both tRNA and amino acid substrates.

Purpose of the Study:

  • To elucidate the molecular basis of amino acid recognition by GlnRS.
  • To determine the structural interactions governing glutamine binding and activation.
  • To investigate the role of tRNA binding in GlnRS substrate specificity.

Main Methods:

  • Synthesis of a stable glutaminyl-adenylate analog inhibitor.

Related Experiment Videos

  • Cocrystallization of GlnRS, tRNA2Gln, and the glutaminyl-adenylate analog.
  • Refinement of the ternary complex crystal structure at 2.4 Å resolution.

    • Main Results:

    • A stable glutaminyl-adenylate analog was synthesized and shown to inhibit GlnRS.
    • The crystal structure of the ternary complex (GlnRS-tRNA2Gln-glutaminyl-adenylate analog) was determined.
    • Key interactions between glutamine and the GlnRS binding site were identified.

    Conclusions:

    • GlnRS distinguishes glutamine from glutamic acid by recognizing both hydrogen atoms on the glutamine sidechain nitrogen.
    • Tyrosine 211 (Tyr211) and a water molecule, acting as hydrogen-bond acceptors, are critical for this specific recognition.
    • tRNA binding, potentially via the terminal nucleotide A76, influences the orientation of Tyr211, facilitating amino acid activation.