Journal
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS
Volume 50, Issue 5, Pages 721-729Publisher
SPRINGER
DOI: 10.1007/s00249-021-01511-x
Keywords
Bacteriophage; Lysins; CBD; Crystal structure
Categories
Funding
- National Nature Science Foundation of China [31770948, 31800159]
- Special Open Fund of Key Laboratory of Experimental Marine Biology, Chinese Academy of Sciences [SKF2020NO1]
- Marine Economic Development Special Fund of Fujian Province [FJHJF-L-2020-2]
- project of University-Industry Cooperation from Fujian Provincial Department of Science and Technology [2020Y4007]
- Natural Science Foundation of Fujian Province [2019J05065]
- High-level personnel introduction grant of Fujian Normal University [Z0210509]
- Fujian Provincial Department of Science and Technology [2020Y4007, 2021H0004]
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This study reveals the crystal structure of Lys170 CBD and its assembly into a tetrameric functional unit, as well as identifies key residues involved in host cell binding, providing a basis for designing efficient lysins targeting Enterococcus faecalis.
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 angstrom resolution. The structure reveals that Lys170 CBDs assemble into a tetrameric functional unit and that each monomer folds into a three-stranded beta-sheet core capped on each side by an alpha-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.
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