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Cu,Zn superoxide dismutase structure from a microbial pathogen establishes a class with a conserved dimer interface.

K T Forest1, P R Langford, J S Kroll

  • 1Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, Mail Drop MB-4, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA. forest@bact.wisc.edu

Journal of Molecular Biology
|February 5, 2000
PubMed
Summary

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Antonie van Leeuwenhoek·2015

Researchers determined the X-ray crystal structure of a key bacterial enzyme, Cu,Zn superoxide dismutase (SOD), from a swine pathogen. This finding reveals structural insights into bacterial SODs and aids in developing new antimicrobial drugs.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Macrophages and neutrophils combat microbial infections using superoxide radicals.
  • Gram-negative bacteria possess periplasmic Cu,Zn superoxide dismutases (SODs) to neutralize superoxide, converting it to oxygen and hydrogen peroxide.

Purpose of the Study:

  • To determine the X-ray crystal structure of Cu,Zn SOD from Actinobacillus pleuropneumoniae, a significant porcine pathogen.
  • To elucidate the structural basis of bacterial Cu,Zn SODs and compare them with eukaryotic counterparts.
  • To identify potential targets for novel antimicrobial drug development.

Main Methods:

  • X-ray crystallography was employed to solve the structure at 1.9 Å resolution.
  • Molecular replacement was used to determine the initial structural model.

Related Experiment Videos

  • Structure-based sequence alignment was performed for bacterial SOD enzymes.

    • Main Results:

    • The dimeric bacterial Cu,Zn SOD enzyme exhibits structural homology with a water-mediated dimer interface.
    • The enzyme shares the Greek-key β-barrel fold common to all Cu,Zn SODs, with active site copper and zinc ions.
    • Structural analysis revealed potential explanations for monomeric bacterial SODs and suggested additional structural classes.

    Conclusions:

    • The determined structure highlights key differences and similarities between eukaryotic and prokaryotic Cu,Zn SODs.
    • Structural variations among prokaryotic SODs were identified.
    • The findings provide a foundation for designing antimicrobial agents targeting bacterial periplasmic Cu,Zn SODs.