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Beta-lactamases as models for protein-folding studies

M Vanhove1, A Lejeune, R H Pain

  • 1Laboratoire d'Enzymologie, Institut de Chimie, Sart Tilman, Liège, Belgium. marc.vanhove@stjude.org

Cellular and Molecular Life Sciences : CMLS
|June 6, 1998
PubMed
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This review examines beta-lactamase folding, revealing transient states and multiphasic kinetics. Key findings include proline isomerization and omega-loop packing as crucial steps in protein folding.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biology

Background:

  • Beta-lactamases are crucial enzymes with complex folding pathways.
  • Understanding protein folding is fundamental to molecular biology and drug development.
  • Previous studies have identified equilibrium and transient condensed states in protein folding.

Purpose of the Study:

  • To review key features of beta-lactamase folding.
  • To elucidate the relevance of beta-lactamase folding to general protein folding principles.
  • To highlight the role of intermediates and specific conformational changes in the folding process.

Main Methods:

  • Analysis of kinetic data, including acrylamide quenching of tryptophan fluorescence.
  • Examination of X-ray crystallographic studies of beta-lactamase and its mutants.

Related Experiment Videos

  • Review of studies on TEM-1 beta-lactamase and Staphylococcus aureus beta-lactamase.

    • Main Results:

    • Protein folding kinetics are multiphasic, involving early transient nonnative intermediates.
    • Intermediate folding phases reflect progressive folding of different molecular regions.
    • Late folding stages involve proline isomerization and omega-loop collapse and packing.

    Conclusions:

    • Beta-lactamase folding provides insights into general protein folding mechanisms.
    • Transient condensed states and specific isomerization events are critical for achieving the native protein structure.
    • The final folding step involves the precise arrangement of structural elements like the omega-loop.