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Related Experiment Videos

Tiny TIM: a small, tetrameric, hyperthermostable triosephosphate isomerase.

H Walden1, G S Bell, R J Russell

  • 1Centre for Biomolecular Sciences, The University of St Andrews, Fife, KY16 9ST, Scotland.

Journal of Molecular Biology
|March 13, 2001
PubMed
Summary
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The hyperthermophilic archaeon Pyrococcus woesei TIM enzyme forms a stable tetramer, unlike typical dimeric forms. This tetrameric structure, with pruned helices and a compact monomer, enhances extreme thermal stability.

Area of Science:

  • Structural biology
  • Biochemistry
  • Extremophile research

Background:

  • Protein thermoadaptation mechanisms are studied in organisms with diverse growth optima.
  • Higher oligomeric states can contribute to protein hyperthermostability.
  • Triosephosphate isomerase (TIM) is a common enzyme, typically existing as a dimer.

Purpose of the Study:

  • To determine the crystal structure of TIM from the hyperthermophilic archaeon Pyrococcus woesei.
  • To investigate the structural basis for extreme thermostability in P. woesei TIM.
  • To compare the structure of hyperthermophilic TIM with less thermostable homologues.

Main Methods:

  • X-ray crystallography at 2.7 A resolution.
  • Comparative structural analysis of TIM enzymes.

Related Experiment Videos

  • Analysis of protein oligomerization and monomeric structure.

    • Main Results:

    • The first archaeal TIM structure was determined for P. woesei TIM, revealing a tetrameric form.
    • P. woesei TIM monomers are smaller and more compact due to pruned helices and truncated loops compared to mesophilic TIMs.
    • The tetramer is formed by extensive hydrophobic interactions between two conserved TIM dimers, stabilizing the structure.

    Conclusions:

    • Extreme thermostability in P. woesei TIM is achieved through a compact tetrameric assembly.
    • The formation of a tetramer via hydrophobic interactions, involving pruned helical regions, enhances stability.
    • Higher oligomerization states play a significant role in extreme thermal stabilization of proteins.