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Related Experiment Videos

Outer-membrane phospholipase A: known structure, unknown biological function.

N Dekker1

  • 1Department of Enzymology and Protein Engineering, Center for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. n.dekker@chem.uu.nl

Molecular Microbiology
|February 26, 2000
PubMed
Summary
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Outer-membrane phospholipase A (OMPLA) activity is regulated by dimerization, which is induced by membrane changes. Structural insights reveal how OMPLA activation occurs, impacting bacterial cell envelope integrity and pathogenicity.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Outer-membrane phospholipase A (OMPLA) is a key enzyme in Gram-negative bacteria's outer membrane.
  • OMPLA activity is tightly regulated to prevent phospholipid degradation.

Purpose of the Study:

  • To elucidate the structural basis of OMPLA regulation and activation.
  • To understand the mechanism of OMPLA-mediated phospholipid hydrolysis.

Main Methods:

  • Analysis of crystal structures of monomeric and dimeric OMPLA.
  • Biochemical characterization of OMPLA catalytic activity.

Main Results:

  • OMPLA activation requires dimerization, forming functional substrate binding sites.

Related Experiment Videos

  • Membrane perturbation induces non-bilayer structures, promoting OMPLA dimerization and activity.
  • A unique Asn-156-His-142-Ser-144 catalytic triad was identified.

    • Conclusions:

    • Membrane perturbation is a key trigger for OMPLA activation via dimerization.
    • OMPLA plays a role in maintaining cell envelope integrity and bacterial pathogenicity.