6AKV

Crystal structure of LysB4, the endolysin from Bacillus cereus-targeting bacteriophage B4

6AKV の概要

• エントリーDOI: 10.2210/pdb6akv/pdb
• 分子名称: LysB4, ZINC ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: endolysin, las type enzyme, l-alanoyl d-glutamate endopeptidase, hydrolase
• 由来する生物種: Bacillus phage B4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30280.20

構造登録者

Hong, S.,Ha, N.-C. (登録日: 2018-09-03, 公開日: 2019-02-13, 最終更新日: 2023-11-22)

主引用文献

Hong, S.,Son, B.,Ryu, S.,Ha, N.C.
Crystal Structure of LysB4, an Endolysin fromBacillus cereus-Targeting Bacteriophage B4.
Mol. Cells, 42:79-86, 2019

PubMed 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 -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 -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 Zn 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 -infecting phages.

PubMed: 30518175
DOI: 10.14348/molcells.2018.0379

実験手法

X-RAY DIFFRACTION (2.4 Å)