2as9
From Proteopedia
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Functional and structural characterization of Spl proteases from staphylococcus aureus
Overview
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.
About this Structure
2AS9 is a Single protein structure of sequence from Staphylococcus aureus with as ligand. 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
Page seeded by OCA on Tue Jan 29 18:08:52 2008
