1bqb: Difference between revisions

Revision as of 19:31, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bqb.png

Template:STRUCTURE 1bqb

AUREOLYSIN, STAPHYLOCOCCUS AUREUS METALLOPROTEINASEAUREOLYSIN, STAPHYLOCOCCUS AUREUS METALLOPROTEINASE

Template:ABSTRACT PUBMED 9753696

About this StructureAbout this Structure

1BQB is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-'''AUREOLYSIN, STAPHYLOCOCCUS AUREUS METALLOPROTEINASE'''
+===AUREOLYSIN, STAPHYLOCOCCUS AUREUS METALLOPROTEINASE===
-==Overview==
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-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.
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+{{ABSTRACT_PUBMED_9753696}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Metalloproteinase]]
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