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From Proteopedia
Structure of ESP, serine protease from Staphylococcus epidermidis
Structural highlights
FunctionGSEA_STAES Exhibits a significant hydrolytic activity for the carbonyl side of glutamic acid. Shows activity toward human fibronectin and type 1 collagen (By similarity). Publication Abstract from PubMedStaphylococcus epidermidis, a commensal of humans, secretes Esp protease to prevent Staphylococcus aureus biofilm formation and colonization. Blocking S. aureus colonization may reduce the incidence of invasive infectious diseases; however, the mechanism whereby Esp disrupts biofilms is unknown. We show here that Esp cleaves autolysin (Atl)-derived murein hydrolases and prevents staphylococcal release of DNA, which serves as extracellular matrix in biofilms. The three-dimensional structure of Esp was revealed by x-ray crystallography and shown to be highly similar to that of S. aureus V8 (SspA). Both atl and sspA are necessary for biofilm formation, and purified SspA cleaves Atl-derived murein hydrolases. Thus, S. aureus biofilms are formed via the controlled secretion and proteolysis of autolysin, and this developmental program appears to be perturbed by the Esp protease of S. epidermidis. Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus.,Chen C, Krishnan V, Macon K, Manne K, Narayana SV, Schneewind O J Biol Chem. 2013 Oct 11;288(41):29440-52. doi: 10.1074/jbc.M113.502039. Epub, 2013 Aug 22. PMID:23970550[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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