Crystal Structure of LysB4, an Endolysin from Bacillus cereus-Targeting Bacteriophage B4
Seokho Hong1,2, Bokyung Son1,2, Sangryeol Ryu1,*, and Nam-Chul Ha1,*
1Department of Agricultural Biotechnology, Research Institute of Agriculture and Life Sciences, Center for Food and Bioconvergence, Center for Food Safety and Toxicology, Seoul National University, Seoul 08826, Korea, 2These authors contributed equally to this work.
*Correspondence: sangryu@snu.ac.kr (SR); hanc210@snu.ac.kr (NCH)
Received September 20, 2018; Revised October 30, 2018; Accepted November 11, 2018.; Published online December 5, 2018.
© Korean Society for Molecular and Cellular Biology. All rights reserved.

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ABSTRACT
Endolysins are bacteriophage-derived enzymes that hydrolyze the peptidoglycan of host bacteria. Endolysins are considered to be promising tools for the control of pathogenic bacteria. LysB4 is an endolysin produced by Bacillus cereus-infecting bacteriophage B4, and consists of an N-terminal enzymatic active domain (EAD) and a C-terminal cell wall binding domain (CBD). LysB4 was discovered for the first time as an Lalanoyl-D-glutamate endopeptidase with the ability to breakdown the peptidoglycan among B. cereus-infecting phages. To understand the activity of LysB4 at the molecular level, this study determined the X-ray crystal structure of the LysB4 EAD, using the full-length LysB4 endolysin. The LysB4 EAD has an active site that is typical of LAS-type enzymes, where Zn2+ is tetrahedrally coordinated by three amino acid residues and one water molecule. Mutational studies identified essential residues that are involved in lytic activity. Based on the structural and biochemical information about LysB4, we suggest a ligand-docking model and a putative endopeptidase mechanism for the LysB4 EAD. These suggestions add insight into the molecular mechanism of the endolysin LysB4 in B. cereusinfecting phages.
Keywords:
Bacillus cereus, bacteriophage B4, endolysin, LAStype enzyme, L-alanoyl D-glutamate endopeptidase


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30 November 2018 Volume 41,
Number 11, pp. 933~992

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