1bqb

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(New page: 200px<br /><applet load="1bqb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqb, resolution 1.72&Aring;" /> '''AUREOLYSIN, STAPHYLO...)
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Revision as of 09:42, 20 November 2007

Image:1bqb.jpg

1bqb, resolution 1.72Å

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AUREOLYSIN, STAPHYLOCOCCUS AUREUS METALLOPROTEINASE

Overview

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, beta-strand-rich upper domain and an alpha-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.

About this Structure

1BQB is a Single protein structure of sequence from Staphylococcus aureus with ZN and CA as ligands. Active as Thermolysin, with EC number 3.4.24.27 Full crystallographic information is available from OCA.

Reference

Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution., Banbula A, Potempa J, Travis J, Fernandez-Catalan C, Mann K, Huber R, Bode W, Medrano F, Structure. 1998 Sep 15;6(9):1185-93. PMID:9753696

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