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Related Experiment Videos

Refinement and structural analysis of barnase at 1.5 A resolution.

C Martin1, V Richard, M Salem

  • 1Laboratoire de Physique, CNRS, ERS 582, Centre d'Etudes Pharmaceutiques, 92296 Châtenay-Malabry CEDEX, France.

Acta Crystallographica. Section D, Biological Crystallography
|March 25, 1999
PubMed
Summary

High-resolution structural analysis of Bacillus amyloliquefaciens ribonuclease (barnase) reveals key water molecules and a Zn2+ ion mediating interactions. This refined barnase structure aids understanding of enzyme-inhibitor binding, particularly with barstar.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Bacillus amyloliquefaciens ribonuclease (barnase) is an extracellular enzyme with a known structure.
  • Previous structural studies provided initial insights into barnase and its interactions.

Purpose of the Study:

  • To refine the high-resolution structure of barnase.
  • To analyze the role of solvent molecules and identify metal ions in barnase structure and interactions.

Main Methods:

  • X-ray crystallography with synchrotron radiation.
  • Refinement using anisotropic atomic displacement parameters.
  • Analysis of solvent structure and molecular interactions.

Main Results:

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  • Achieved a 1.5 A resolution structure with R factor 11.5% and Rfree 17.4%.
  • Identified 16 equivalent buried water molecules and their structural roles.
  • Discovered a Zn2+ ion mediating contacts between symmetry-related barnase molecules.

    • Conclusions:

    • The refined barnase structure provides enhanced accuracy for detailed analysis.
    • Water molecules play a crucial role in barnase-barstar interactions.
    • The Zn2+ ion's mediation of inter-molecular contacts is a significant finding.