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Related Experiment Videos

Wild-type and E106Q mutant carbonic anhydrase complexed with acetate.

K Håkansson1, C Briand, V Zaitsev

  • 1Molecular Biophysics, Chemical Center, University of Lund, Sweden.

Acta Crystallographica. Section D, Biological Crystallography
|January 1, 1994
PubMed
Summary

Structural analysis of human carbonic anhydrase II (HCAII) reveals how a mutation alters inhibitor binding. The E106Q mutant shows unique hydrogen bonding interactions not present in wild-type HCAII.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Human carbonic anhydrase II (HCAII) is a crucial enzyme involved in various physiological processes.
  • Understanding enzyme-inhibitor interactions is key to developing targeted therapeutics.
  • The active site's hydrogen-bond network plays a vital role in enzyme function.

Purpose of the Study:

  • To elucidate the molecular structures of wild-type HCAII and its E106Q mutant in complex with acetate.
  • To investigate the impact of the E106Q mutation on inhibitor binding and active site interactions.
  • To analyze the differences in hydrogen-bonding patterns between the wild-type and mutant enzyme complexes.

Main Methods:

  • X-ray crystallography was employed to solve the molecular structures.

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  • High-resolution data (2.1 Å for wild-type, 1.9 Å for mutant) were obtained.
  • Crystallographic data were analyzed to determine atomic coordinates and hydrogen-bonding networks.

    • Main Results:

    • The acetate complexes of wild-type HCAII and the E106Q mutant were determined to high resolution.
    • The E106Q mutation altered the active site hydrogen-bond network.
    • A unique hydrogen bond interaction between a carboxylate oxygen and Thr199 Oγ1 was observed in the mutant, but not the wild-type complex.

    Conclusions:

    • The E106Q mutation significantly influences inhibitor binding through altered active site hydrogen bonding.
    • This discrimination in binding interactions highlights the importance of specific residues in enzyme catalysis.
    • The findings provide insights into the structure-function relationship of HCAII and potential drug design strategies.