4JCN

Structure of ESP, serine protease from Staphylococcus epidermidis

4JCN の概要

• エントリーDOI: 10.2210/pdb4jcn/pdb
• 分子名称: Glutamyl endopeptidase (2 entities in total)
• 機能のキーワード: extracellular serine protease, esp, biofilm, glutamyl endopeptidase, protease, hydrolase
• 由来する生物種: Staphylococcus epidermidis
• 細胞内の位置: Secreted (By similarity): P0C0Q2
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23602.10

構造登録者

Krishnan, V.,Sthanam, V.L.N. (登録日: 2013-02-22, 公開日: 2013-09-04, 最終更新日: 2023-11-08)

主引用文献

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

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: 23970550
DOI: 10.1074/jbc.M113.502039

実験手法

X-RAY DIFFRACTION (1.8 Å)