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Related Experiment Videos

Substrate-induced interconversion of protein quaternary structure isoforms.

Lei Tang1, Linda Stith, Eileen K Jaffe

  • 1Fox Chase Cancer Center, Philadelphia, Pennsylvania 19111, USA.

The Journal of Biological Chemistry
|February 16, 2005
PubMed
Summary
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Human porphobilinogen synthase (PBGS) exists in two forms, an octamer and a hexamer. Ligand interactions at the active site drive structural changes, favoring the high-activity octamer form.

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Human porphobilinogen synthase (PBGS) exhibits dynamic equilibrium between two quaternary structure isoforms.
  • These isoforms, a high-activity octamer and a low-activity hexamer, arise from distinct monomer conformations.

Purpose of the Study:

  • To investigate the role of enzyme active site interactions in mediating the structural interconversion of PBGS isoforms.
  • To determine if ligand binding influences the equilibrium between PBGS quaternary structures.

Main Methods:

  • Enzyme kinetics studies.
  • Analysis of protein quaternary structure.
  • Ligand binding assays.

Main Results:

Related Experiment Videos

  • Ligand interactions at the PBGS active site were shown to promote structural interconversion.
  • The binding of ligands favors the formation of the high-activity octameric structure over the hexameric form.

    • Conclusions:

    • Enzymatic catalysis and associated protein motions can facilitate the assembly and disassembly of oligomeric proteins.
    • Ligand interactions are key regulators of PBGS quaternary structure and activity.