1bqb
From Proteopedia
(New page: 200px<br /><applet load="1bqb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bqb, resolution 1.72Å" /> '''AUREOLYSIN, STAPHYLO...) |
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| - | [[Image:1bqb.jpg|left|200px]]<br /><applet load="1bqb" size=" | + | [[Image:1bqb.jpg|left|200px]]<br /><applet load="1bqb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bqb, resolution 1.72Å" /> | caption="1bqb, resolution 1.72Å" /> | ||
'''AUREOLYSIN, STAPHYLOCOCCUS AUREUS METALLOPROTEINASE'''<br /> | '''AUREOLYSIN, STAPHYLOCOCCUS AUREUS METALLOPROTEINASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: Aureolysin is an extracellular zinc-dependent | + | 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== | ==About this Structure== | ||
| - | 1BQB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] Full crystallographic information is available from [http:// | + | 1BQB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BQB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Banbula, A.]] | [[Category: Banbula, A.]] | ||
[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
| - | [[Category: Medrano, F | + | [[Category: Medrano, F J.]] |
[[Category: Potempa, J.]] | [[Category: Potempa, J.]] | ||
[[Category: Travis, J.]] | [[Category: Travis, J.]] | ||
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[[Category: metalloproteinase]] | [[Category: metalloproteinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:57:59 2008'' |
Revision as of 09:58, 21 February 2008
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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 and 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
Page seeded by OCA on Thu Feb 21 11:57:59 2008
Categories: Single protein | Staphylococcus aureus | Thermolysin | Banbula, A. | Bode, W. | Medrano, F J. | Potempa, J. | Travis, J. | CA | ZN | Hydrolase | Metalloproteinase
