7D55

Crystal structure of lys170 CBD

7D55 の概要

• エントリーDOI: 10.2210/pdb7d55/pdb
• 分子名称: Putative N-acetylmuramoyl-L-alanine amidase (2 entities in total)
• 機能のキーワード: lysin, hydrolase
• 由来する生物種: Enterococcus phage phiM1EF22
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 41563.58

構造登録者

Zhen, X. (登録日: 2020-09-25, 公開日: 2021-06-09, 最終更新日: 2024-03-27)

主引用文献

Xu, X.,Zhang, D.,Zhou, B.,Zhen, X.,Ouyang, S.
Structural and biochemical analyses of the tetrameric cell binding domain of Lys170 from enterococcal phage F170/08.
Eur.Biophys.J., 50:721-729, 2021

PubMed Abstract: Lysins are a class of hydrolytic enzymes used by bacteriophages to target and cleave the peptidoglycan of bacterial cell walls during their lytic cycle. The lysins from bacteriophages that infect Gram-positive bacteria are typically monomeric and consist of one or two catalytic domains (CD) and a cell binding domain (CBD). However, multimeric lysins encoded by a single gene have also been reported, among which Lys170 from enterococcal phage F170/08 was one of the first identified. Here, we determined the crystal structure of Lys170 CBD at 1.40 Å resolution. The structure reveals that Lys170 CBDs assemble into a tetrameric functional unit and that each monomer folds into a three-stranded β-sheet core capped on each side by an α-helix. In addition, we identified key residues of Lys170 CBD involved in host cell binding. Our work provides a basis for designing highly efficient lysins targeting Enterococcus faecalis.

PubMed: 33609147
DOI: 10.1007/s00249-021-01511-x

実験手法

X-RAY DIFFRACTION (1.397 Å)