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Related Experiment Videos

Dynamic allostery in the ring protein TRAP.

Jonathan G Heddle1, Tomoyuki Okajima, David J Scott

  • 1Yokohama City University, Tsurumi, Suehiro 1-7-29, Yokohama 230-0045, Japan. jgh4@tsurumi.yokohama-cu.ac.jp

Journal of Molecular Biology
|June 15, 2007
PubMed
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We found distinct thermodynamic differences in how tryptophan binds to TRAP proteins from different bacteria. A single amino acid change in Bacillus subtilis TRAP protein alters tryptophan binding cooperativity.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Microbiology

Background:

  • The trp RNA-binding attenuation protein (TRAP) regulates gene expression in bacteria.
  • TRAP functions as an 11-mer ring, binding 11 tryptophan molecules at symmetry-related sites.

Purpose of the Study:

  • To investigate the thermodynamic differences in tryptophan binding by TRAP from different bacterial species.
  • To identify the molecular basis for altered ligand binding cooperativity in Bacillus subtilis TRAP.

Main Methods:

  • Isothermal titration calorimetry (ITC) was used to analyze tryptophan binding thermodynamics.
  • Site-directed mutagenesis was employed to identify key amino acid residues.

Main Results:

  • Tryptophan binding to Bacillus stearothermophilus TRAP is non-cooperative.

Related Experiment Videos

  • Bacillus subtilis TRAP exhibits cooperative tryptophan binding, with initial ligand binding affecting subsequent interactions.
  • A single Ile to Leu substitution in B. subtilis TRAP abolishes this cooperative binding effect.

    • Conclusions:

    • Distinct thermodynamic signatures exist for tryptophan binding to TRAP across bacterial species.
    • A conserved amino acid residue plays a critical role in mediating cooperative ligand binding in B. subtilis TRAP.
    • Ligand binding can induce conformational changes propagating through the TRAP protein ring.