2NW0

Crystal structure of a lysin

Summary for 2NW0

• Entry DOI: 10.2210/pdb2nw0/pdb
• Descriptor: PlyB, ACETATE ION (3 entities in total)
• Functional Keywords: beta barrel, hydrolase
• Biological source: unidentified phage
• Total number of polymer chains: 2
• Total formula weight: 43386.46

Authors

Porter, C.J.,Buckle, A.M.,Whisstock, J.C. (deposition date: 2006-11-14, release date: 2006-12-05, Last modification date: 2023-10-25)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.6 Å)