Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A

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A Banbula1, J Potempa, J Travis

  • 1Jagiellonian University Institute of Molecular Biology Al. Mickiewicza 3, 31-120, Krakow, Poland.

Structure (London, England : 1993)
|October 1, 1998
PubMed
Abstract

Insights

Aureolysin, a Staphylococcus aureus metalloproteinase, has a unique "closed" active site structure. This finding challenges the universal model for neutral metalloproteinase hinge motion.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Aureolysin is an extracellular zinc-dependent metalloproteinase from Staphylococcus aureus.
  • It plays a role in staphylococcal disease pathology due to its activity against host molecules.

Purpose of the Study:

  • To determine the amino acid sequence and X-ray crystal structure of aureolysin.
  • To compare the structure of aureolysin with other known metalloproteinases.

Main Methods:

  • X-ray crystallography
  • Amino acid sequencing

Main Results:

  • The inhibitor-free X-ray crystal structure of aureolysin was determined.
  • Aureolysin comprises 301 amino acids with distinct beta-strand-rich and alpha-helix-rich domains, binding one zinc and three calcium ions.
  • Unlike other family members, aureolysin exhibits a 'closed' active site cleft conformation.

Conclusions:

  • The structure of aureolysin is highly similar to thermolysin, neutral protease, and elastase.
  • The 'closed' active site conformation of aureolysin raises questions about the hinge-bending motion model in neutral metalloproteinases.
  • This discovery offers new insights into metalloproteinase structural dynamics and function.

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