4JCN
Structure of ESP, serine protease from Staphylococcus epidermidis
Summary for 4JCN
| Entry DOI | 10.2210/pdb4jcn/pdb |
| Descriptor | Glutamyl endopeptidase (2 entities in total) |
| Functional Keywords | extracellular serine protease, esp, biofilm, glutamyl endopeptidase, protease, hydrolase |
| Biological source | Staphylococcus epidermidis |
| Cellular location | Secreted (By similarity): P0C0Q2 |
| Total number of polymer chains | 1 |
| Total formula weight | 23602.10 |
| Authors | Krishnan, V.,Sthanam, V.L.N. (deposition date: 2013-02-22, release date: 2013-09-04, Last modification date: 2023-11-08) |
| Primary citation | Chen, C.,Krishnan, V.,Macon, K.,Manne, K.,Narayana, S.V.,Schneewind, O. Secreted proteases control autolysin-mediated biofilm growth of Staphylococcus aureus J.Biol.Chem., 288:29440-29452, 2013 Cited by PubMed Abstract: Staphylococcus 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. PubMed: 23970550DOI: 10.1074/jbc.M113.502039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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