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Trimeric domain-swapped barnase

I Zegers1, J Deswarte, L Wyns

  • 1Laboratorium voor Ultrastructuur, Vrije Universiteit Brussel, Vlaams Interuniversitair Instituut voor Biotechnologie, Paardenstraat 65, B-1640 St. Genesius Rode, Belgium. igzegers@vub.ac.be

Proceedings of the National Academy of Sciences of the United States of America
|February 3, 1999
PubMed
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The structure of trimeric barnase reveals domain swapping, where parts of one protein molecule bind to another. This finding supports existing models of barnase protein folding.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Folding

Background:

  • Barnase is a ribonuclease enzyme.
  • Protein folding can involve complex mechanisms, including domain swapping.
  • Understanding protein structure is crucial for biological function.

Purpose of the Study:

  • To determine the three-dimensional structure of a trimeric domain-swapped form of barnase.
  • To elucidate the mechanism of domain swapping in barnase.

Main Methods:

  • X-ray crystallography was employed to determine the structure.
  • Data were collected at a resolution of 2.2 Å.
  • Crystals belonged to space group R32.

Main Results:

Related Experiment Videos

  • A cyclic trimer of barnase was identified, exhibiting domain swapping.
  • Specific residues (1-36 and 41-110) from different molecules associate.
  • The swapped domains contain nucleation sites essential for folding.

    • Conclusions:

    • The observed trimeric structure provides insights into barnase's quaternary structure.
    • Domain swapping in barnase is consistent with a foldon-based folding model.
    • This study enhances our understanding of protein folding pathways and alternative conformations.