1YB0

Structure of PlyL

Summary for 1YB0

• Entry DOI: 10.2210/pdb1yb0/pdb
• Descriptor: prophage LambdaBa02, N-acetylmuramoyl-L-alanine amidase, family 2, ZINC ION, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: n-acetylmuramoyl-l-alanine amidase, plyl, e.c.3.5.1.28, hydrolase
• Biological source: Bacillus anthracis
• Total number of polymer chains: 3
• Total formula weight: 54755.46

Authors

Low, L.Y.,Yang, C.,Perego, M.,Osterman, A.,Liddington, R.C. (deposition date: 2004-12-18, release date: 2005-08-23, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.86 Å)