Structure
Volume 6, Issue 9, 15 September 1998, Pages 1185-1193
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Research Article
Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 å resolution

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Abstract

Background: Aureolysin is an extracellular zinc-dependent metalloproteinase from the pathogenic bacterium Staphylococcus aureus. This enzyme exhibits in vitro activity against several molecules of biological significance for the host, indicating that it is involved in the pathology of staphylococcal diseases.

Results: Here we report the amino-acid sequence and inhibitor-free X-ray crystal structure of aureolysin, a member of the thermolysin family of zinc-dependent metalloproteinases. This enzyme, which binds one zinc and three calcium ions, comprises a single chain of 301 amino acids that consists of a β-strand-rich upper domain and an α-helix-rich lower domain.

Conclusions: The overall structure of aureolysin is very similar to that of the other three members of this family whose structures are known – thermolysin (TLN) from Bacillus thermoproteolyticus, neutral protease (NP) from Bacillus cereus and elastase (PAE) from Pseudomonas aeruginosa. But an important difference has been encountered: in contrast to what has been observed in the other three members of this family (TLN, NP and PAE), inhibitor-free aureolysin displays a ‘closed’ active site cleft conformation. This new structure therefore raises questions about the universality of the hinge-bending motion model for the neutral metalloproteinases.

Keywords

aureolysin
metalloproteinases
Staphylococcus aureus
thermolysin

Cited by (0)

A Banbula and J Potempa, Jagiellonian University, Institute of Molecular Biology, Al. Mickiewicza 3, 31-120, Krakow, Poland.

J Travis, Department of Biochemistry, The University of Georgia, Athens, GA 30602, USA.

C Fernandez-Catalán, K Mann, R Huber, W Bode and F Medrano, Max-Plank-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18a, D-82152, Martinsried, Germany.

Present address for F Medrano (corresponding author): C.I.B. (C.S.I.C.), C/ Velázquez 144, 28006 - Madrid, Spain. e-mail: [email protected].