4DNY

Crystal structure of enterohemorrhagic E. coli StcE(132-251)

4DNY の概要

• エントリーDOI: 10.2210/pdb4dny/pdb
• 関連するPDBエントリー: 3UJZ
• 分子名称: Metalloprotease stcE, IODIDE ION (3 entities in total)
• 機能のキーワード: metzincin, bacterial zinc metalloprotease, o-linked glycoprotein, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Secreted: O82882
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14637.60

構造登録者

Yu, A.C.Y.,Strynadka, N.C.J. (登録日: 2012-02-09, 公開日: 2012-05-16, 最終更新日: 2024-02-28)

主引用文献

Yu, A.C.,Worrall, L.J.,Strynadka, N.C.
Structural Insight into the Bacterial Mucinase StcE Essential to Adhesion and Immune Evasion during Enterohemorrhagic E. coli Infection.
Structure, 20:707-717, 2012

PubMed Abstract: Mucin glycoproteins with large numbers of O-linked glycosylations comprise the mucosal barrier lining the mammalian gastrointestinal tract from mouth to gut. A critical biological function of mucins is to protect the underlying epithelium from infection. Enterohemorrhagic Escherichia coli (EHEC), the mediator of severe food- and water-borne disease, can breach this barrier and adhere to intestinal cells. StcE, a ∼100 kDa metalloprotease secreted by EHEC, plays a pivotal role in remodeling the mucosal lining during infection. To obtain mechanistic insight into its function, we have determined the structure of StcE. Our data reveal a dynamic, multidomain architecture featuring an unusually large substrate-binding cleft and a prominent polarized surface charge distribution highly suggestive of an electrostatic role in substrate targeting. The observation of key conserved motifs in the active site allows us to propose the structural basis for the specific recognition of α-O-glycan-containing substrates. Complementary biochemical analysis provides further insight into its distinct substrate specificity and binding stoichiometry.

PubMed: 22483117
DOI: 10.1016/j.str.2012.02.015

実験手法

X-RAY DIFFRACTION (1.61 Å)