ArticleEuropean biophysics journal : EBJ2021
Structural and biochemical analyses of the tetrameric cell binding domain of Lys170 from enterococcal phage F170/08.
Article in European biophysics journal : EBJ, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Data mining reveals the diversity of prophage endolysins targeting pathogenic enterococci.The Journal of general virology · 2026Article
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- A review and new perspective on oral bacteriophages: manifestations in the ecology of oral diseases.Journal of oral microbiology · 2024Review
- Development of a Magnetic Bead-Based Method for Specific Detection ofJournal of microbiology and biotechnology · 2023Article
- Prophage-Derived Regions inInternational journal of molecular sciences · 2023Article
- Characterization of an isolated lactase enzyme produced byFrontiers in microbiology · 2023Article
- On the Occurrence and Multimerization of Two-Polypeptide Phage Endolysins Encoded in Single Genes.Microbiology spectrum · 2022Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
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.
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