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| - | [[Image:2as9.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2as9| PDB=2as9 | SCENE= }} | | {{STRUCTURE_2as9| PDB=2as9 | SCENE= }} |
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| - | '''Functional and structural characterization of Spl proteases from staphylococcus aureus'''
| + | ===Functional and structural characterization of Spl proteases from staphylococcus aureus=== |
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| - | ==Overview==
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| - | Staphylococcus aureus is the major cause of nosocomial infections world-wide, with increasing prevalence of community-acquired diseases. The recent dramatic increase in multi-antibiotic resistance, including resistance to the last-resort drug, vancomycin, together with the lack of an effective vaccine highlight the need for better understanding of S.aureus pathogenicity. Comparative analysis of available bacterial genomes allows for the identification of previously uncharacterized S.aureus genes with potential roles in pathogenicity. A good example is a cluster of six serine protease-like (spl) genes encompassed in one operon, which encode for putative proteases with similarity to staphylococcal glutamylendopeptidase (V8 protease). Here, we describe an efficient expression system for the production of recombinant SplB and SplC proteases in Escherichia coli, together with structural and functional characterization of the purified enzymes. A unique mechanism of cytoplasm protection against activity of misdirected SplB was uncovered. Apparently, the co-translated signal peptide maintains protease latency until it is cleaved by the signal peptidase during protein secretion. Furthermore, the crystal structure of the SplC protease revealed a fold resembling that of the V8 protease and epidermolytic toxins. Arrangement of the active site cleft and substrate-binding pocket of SplC explains the mechanism of enzyme latency and suggests that some Spl proteases possess restricted substrate specificity similar to that of the V8 protease and epidermolytic toxins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16516230}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16516230 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16516230}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Staphylococcus aureus]] | | [[Category: Staphylococcus aureus]] |
| | [[Category: Trypsin-like fold]] | | [[Category: Trypsin-like fold]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:25:05 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:09:24 2008'' |
Revision as of 04:09, 28 July 2008
Template:STRUCTURE 2as9
Functional and structural characterization of Spl proteases from staphylococcus aureus
Template:ABSTRACT PUBMED 16516230
About this Structure
2AS9 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Functional and structural characterization of Spl proteases from Staphylococcus aureus., Popowicz GM, Dubin G, Stec-Niemczyk J, Czarny A, Dubin A, Potempa J, Holak TA, J Mol Biol. 2006 Apr 21;358(1):270-9. Epub 2006 Feb 13. PMID:16516230
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