1XJT

Crystal structure of active form of P1 phage endolysin Lyz

1XJT の概要

• エントリーDOI: 10.2210/pdb1xjt/pdb
• 関連するPDBエントリー: 1XJU
• 分子名称: Lysozyme, CITRIC ACID (3 entities in total)
• 機能のキーワード: open conformation, hydrolase
• 由来する生物種: Enterobacteria phage P1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21871.60

構造登録者

Arockiasamy, A.,Sacchettini, J.C. (登録日: 2004-09-24, 公開日: 2005-01-11, 最終更新日: 2024-10-09)

主引用文献

Xu, M.,Arulandu, A.,Struck, D.K.,Swanson, S.,Sacchettini, J.C.,Young, R.
Disulfide isomerization after membrane release of its SAR domain activates P1 lysozyme.
Science, 307:113-117, 2005

PubMed Abstract: The P1 lysozyme Lyz is secreted to the periplasm of Escherichia coli and accumulates in an inactive membrane-tethered form. Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. Crystal structures confirm the alternative disulfide linkages in the two forms of Lyz and reveal dramatic conformational differences in the catalytic domain. Thus, the exported P1 endolysin is kept inactive by three levels of control-topological, conformational, and covalent-until its release from the membrane is triggered by the P1 holin.

PubMed: 15637279
DOI: 10.1126/science.1105143

実験手法

X-RAY DIFFRACTION (1.75 Å)