4DCB

Y. pestis Plasminogen Activator Pla in Complex with Human Plasminogen Activation Loop Peptide ALP11

これはPDB形式変換不可エントリーです。

4DCB の概要

• エントリーDOI: 10.2210/pdb4dcb/pdb
• 分子名称: Coagulase/fibrinolysin, Plasminogen, (4R)-2-METHYLPENTANE-2,4-DIOL, ... (7 entities in total)
• 機能のキーワード: beta barrel, plasminogen activator, protease, outer membrane, hydrolase
• 由来する生物種: Yersinia pestis; 詳細
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein (By similarity): P17811; Secreted: P00747
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35498.15

構造登録者

Eren, E.,van den Berg, B. (登録日: 2012-01-17, 公開日: 2012-06-06, 最終更新日: 2024-11-27)

主引用文献

Eren, E.,van den Berg, B.
Structural basis for activation of an integral membrane protease by lipopolysaccharide.
J.Biol.Chem., 287:23971-23976, 2012

PubMed Abstract: Omptins constitute a unique family of outer membrane proteases that are widespread in Enterobacteriaceae. The plasminogen activator (Pla) of Yersinia pestis is an omptin family member that is very important for development of both bubonic and pneumonic plague. The physiological function of Pla is to cleave (activate) human plasminogen to form the plasma protease plasmin. Uniquely, lipopolysaccharide (LPS) is essential for the catalytic activity of all omptins, including Pla. Why omptins require LPS for enzymatic activity is unknown. Here, we report the co-crystal structure of LPS-free Pla in complex with the activation loop peptide of human plasminogen, its natural substrate. The structure shows that in the absence of LPS, the peptide substrate binds deep within the active site groove and displaces the nucleophilic water molecule, providing an explanation for the dependence of omptins on LPS for enzymatic activity.

PubMed: 22645135
DOI: 10.1074/jbc.M112.376418

実験手法

X-RAY DIFFRACTION (2.033 Å)