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Related Experiment Videos

The retro-GCN4 leucine zipper sequence forms a stable three-dimensional structure.

P R Mittl1, C Deillon, D Sargent

  • 1Biochemisches Institut der Universität Zürich, Winterthurer Strasse 190, CH-8057 Zürich, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|March 16, 2000
PubMed
Summary

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Protein sequence inversion can lead to stable structures. Researchers determined the crystal structure of retro-GCN4 leucine zipper, revealing a stable four-helix bundle, unlike its natural counterpart.

Area of Science:

  • Protein structure and folding
  • Biochemistry
  • Structural biology

Background:

  • The stability of proteins with inverted natural sequences is a key question in molecular biology.
  • Leucine zippers are known to form stable helical coiled-coils.

Purpose of the Study:

  • To investigate the structural consequences of inverting the natural sequence of the GCN4 leucine zipper.
  • To determine if an inverted protein sequence can adopt a stable fold.

Main Methods:

  • X-ray crystallography was used to determine the 3D structure.
  • The crystal structure was resolved at a resolution of 2.1 angstroms.

Main Results:

  • The retro-GCN4 leucine zipper formed a stable, parallel four-helix bundle.

Related Experiment Videos

  • This structure is distinct from the two-stranded helical coiled-coil of the natural GCN4 leucine zipper.

    • Conclusions:

    • An inverted protein sequence can adopt a stable and distinct fold.
    • The determined structure of the retro-leucine zipper provides a basis for further structural and functional investigations.