2NW0

Crystal structure of a lysin

2NW0 の概要

• エントリーDOI: 10.2210/pdb2nw0/pdb
• 分子名称: PlyB, ACETATE ION (3 entities in total)
• 機能のキーワード: beta barrel, hydrolase
• 由来する生物種: unidentified phage
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43386.46

構造登録者

Porter, C.J.,Buckle, A.M.,Whisstock, J.C. (登録日: 2006-11-14, 公開日: 2006-12-05, 最終更新日: 2023-10-25)

主引用文献

Porter, C.J.,Schuch, R.,Pelzek, A.J.,Buckle, A.M.,McGowan, S.,Wilce, M.C.,Rossjohn, J.,Russell, R.,Nelson, D.,Fischetti, V.A.,Whisstock, J.C.
The 1.6 A Crystal Structure of the Catalytic Domain of PlyB, a Bacteriophage Lysin Active Against Bacillus anthracis.
J.Mol.Biol., 366:540-550, 2007

PubMed Abstract: Lysins are peptidoglycan hydrolases that are produced by bacteriophage and act to lyse the bacterial host cell wall during progeny phage release. Here, we describe the structure and function of a novel bacteriophage-derived lysin, PlyB, which displays potent lytic activity against the Bacillus anthracis-like strain ATCC 4342. This molecule comprises an N-terminal catalytic domain (PlyB(cat)) and a C-terminal bacterial SH3-like domain, SH3b. It is shown that both domains are required for effective catalytic activity against ATCC 4342. Further, PlyB has specific activity comparable to the phage lysin PlyG, an amidase being developed as a therapeutic against anthrax. In contrast to PlyG, however, the 1.6 A X-ray crystal structure of PlyB(cat) reveals that the catalytic domain adopts the glycosyl hydrolase (GH)-25, rather than phage T7 lysozyme-like fold. PlyB therefore represents a new class of anthrax lysin and a new defensive tool in the armament against anthrax-mediated bioterrorism.

PubMed: 17182056
DOI: 10.1016/j.jmb.2006.11.056

実験手法

X-RAY DIFFRACTION (1.6 Å)