2X56

Yersinia Pestis Plasminogen Activator Pla (Native)

2X56 の概要

• エントリーDOI: 10.2210/pdb2x56/pdb
• 関連するPDBエントリー: 2X4M 2X55
• 分子名称: COAGULASE/FIBRINOLYSIN, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total)
• 機能のキーワード: transmembrane, aspartyl protease, cell outer membrane, omptin, protease, hydrolase
• 由来する生物種: YERSINIA PESTIS
• 細胞内の位置: Cell outer membrane ; Multi- pass membrane protein : P17811
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38171.52

構造登録者

Eren, E.,Murphy, M.,Goguen, J.,van den Berg, B. (登録日: 2010-02-05, 公開日: 2010-07-28, 最終更新日: 2024-05-01)

主引用文献

Eren, E.,Murphy, M.,Goguen, J.,van den Berg, B.
An Active Site Water Network in the Plasminogen Activator Pla from Yersinia Pestis
Structure, 18:809-, 2010

PubMed Abstract: The plasminogen activator Pla from Yersinia pestis is an outer membrane protease (omptin) that is important for the virulence of plague. Here, we present the high-resolution crystal structure of wild-type, enzymatically active Pla at 1.9 A. The structure shows a water molecule located between active site residues D84 and H208, which likely corresponds to the nucleophilic water. A number of other water molecules are present in the active site, linking residues important for enzymatic activity. The R211 sidechain in loop L4 is close to the nucleophilic water and possibly involved in the stabilization of the oxyanion intermediate. Subtle conformational changes of H208 result from the binding of lipopolysaccharide to the outside of the barrel, explaining the unusual dependence of omptins on lipopolysaccharide for activity. The Pla structure suggests a model for the interaction with plasminogen substrate and provides a more detailed understanding of the catalytic mechanism of omptin proteases.

PubMed: 20637417
DOI: 10.1016/J.STR.2010.03.013

実験手法

X-RAY DIFFRACTION (2.3 Å)