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Related Experiment Videos

An engineered allosteric switch in leucine-zipper oligomerization

L Gonzalez1, J J Plecs, T Alber

  • 1Department of Molecular and cell Biology, University of California, Berkeley,94720-3206, USA.

Nature Structural Biology
|June 1, 1996
PubMed
Summary

Hydrophobic ligands like benzene can alter protein structure, switching coiled coils between two and three strands. This highlights how core packing influences protein oligomerization specificity and function.

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Area of Science:

  • Protein structure and dynamics
  • Biochemistry and molecular biology
  • Structural biology

Background:

  • The precise role of core side-chain packing in defining protein structure remains debated.
  • Coiled coils are common protein structural motifs involved in various biological processes.

Purpose of the Study:

  • To investigate how core packing influences the oligomeric structure of coiled coils.
  • To engineer a GCN4 leucine zipper mutant that responds to hydrophobic ligands.

Main Methods:

  • Engineering of a GCN4 leucine zipper mutant.
  • Analysis of ligand-induced changes in thermal stability and oligomerization order in solution.
  • X-ray crystallography to determine the structure of the peptide-benzene complex.

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Main Results:

  • The engineered mutant switched from a two-strand to a three-strand oligomer upon binding cyclohexane and benzene.
  • Ligand binding increased the apparent thermal stability and oligomerization order of the leucine zipper.
  • Crystal structure revealed a benzene molecule bound within the core of the trimeric complex.

Conclusions:

  • Coiled coils can function as molecular switches, responding to environmental cues like ligand binding.
  • Core side-chain packing is a critical determinant of oligomerization specificity in coiled coils.
  • This study provides insights into the design principles for creating responsive protein structures.