2AR3

E90A mutant structure of PlyL

2AR3 の概要

• エントリーDOI: 10.2210/pdb2ar3/pdb
• 関連するPDBエントリー: 1YB0
• 分子名称: prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2, ZINC ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: endolysin, hydrolase
• 由来する生物種: Bacillus anthracis
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 54794.59

構造登録者

Low, L.Y.,Yang, C.,Perego, M.,Osterman, A.,Liddington, R.C. (登録日: 2005-08-19, 公開日: 2006-06-06, 最終更新日: 2024-02-14)

主引用文献

Low, L.Y.,Yang, C.,Perego, M.,Osterman, A.,Liddington, R.C.
Structure and lytic activity of a Bacillus anthracis prophage endolysin.
J.Biol.Chem., 280:35433-35439, 2005

PubMed Abstract: We report a structural and functional analysis of the lambda prophage Ba02 endolysin (PlyL) encoded by the Bacillus anthracis genome. We show that PlyL comprises two autonomously folded domains, an N-terminal catalytic domain and a C-terminal cell wall-binding domain. We determined the crystal structure of the catalytic domain; its three-dimensional fold is related to that of the cell wall amidase, T7 lysozyme, and contains a conserved zinc coordination site and other components of the catalytic machinery. We demonstrate that PlyL is an N-acetylmuramoyl-L-alanine amidase that cleaves the cell wall of several Bacillus species when applied exogenously. We show, unexpectedly, that the catalytic domain of PlyL cleaves more efficiently than the full-length protein, except in the case of Bacillus cereus, and using GFP-tagged cell wall-binding domain, we detected strong binding of the cell wall-binding domain to B. cereus but not to other species tested. We further show that a related endolysin (Ply21) from the B. cereus phage, TP21, shows a similar pattern of behavior. To explain these data, and the species specificity of PlyL, we propose that the C-terminal domain inhibits the activity of the catalytic domain through intramolecular interactions that are relieved upon binding of the C-terminal domain to the cell wall. Furthermore, our data show that (when applied exogenously) targeting of the enzyme to the cell wall is not a prerequisite of its lytic activity, which is inherently high. These results may have broad implications for the design of endolysins as therapeutic agents.

PubMed: 16103125
DOI: 10.1074/jbc.M502723200

実験手法

X-RAY DIFFRACTION (2.2 Å)