ArticleScientific reports2019
Structural bases of peptidoglycan recognition by lysostaphin SH3b domain.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 92 citations in OpenAlex.
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- Novel endopeptidase overcoming lysostaphin resistance.Scientific reports · 2026Article
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- A lipid cue drives the subcellular localization of a self-inserting bacterial transmembrane protein.bioRxiv : the preprint server for biology · 2026Article
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- Origin and Evolution of Very Large Extracellular Proteins in Fructophilic Lactic Acid Bacteria.Genome biology and evolution · 2026Article
- Enhancing stability and safety of chimeric peptidoglycan hydrolases by linker engineering.Applied microbiology and biotechnology · 2026Article
- Antibacterial Activity of Bacteriophage Lytic Enzyme Ply900.Veterinary sciences · 2026Article
- A chimeric, half-life extended lysin with a unique mode of action.Frontiers in microbiology · 2026Article
- The New SH3b_T Domain Increases the Structural and Functional Variability Among SH3b-Like CBDs from Staphylococcal Phage Endolysins.Probiotics and antimicrobial proteins · 2025Article
- An Evolutionarily Conserved Laterally Acquired Toolkit Enables Microbiota Targeting by Trichomonas.Molecular biology and evolution · 2025Article
- Archaea produce peptidoglycan hydrolases that kill bacteria.PLoS biology · 2025Article
- Purification and characterization of a novel antibacterial peptide againstMicrobiology (Reading, England) · 2025Article
- ZAM-CS, a novel chimeric endolysin with enhanced stability and rapid action against methicillin-resistant Staphylococcus aureus.BMC microbiology · 2025Article
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- Characterization and bioinformatic analysis of a new chimeric endolysin against MRSA with great stability.AMB Express · 2024Article
- Deleterious Effects of Histidine Tagging to the SH3b Cell Wall-Binding Domain on Recombinant Endolysin Activity.Journal of microbiology and biotechnology · 2024Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Staphylococcus simulans lysostaphin cleaves pentaglycine cross-bridges between stem peptides in the peptidoglycan of susceptible staphylococci, including S. aureus. This enzyme consists of an N-terminal catalytic domain and a cell wall binding domain (SH3b), which anchors the protein to peptidoglycan. Although structures of SH3bs from lysostaphin are available, the binding modes of peptidoglycan to these domains are still unclear. We have solved the crystal structure of the lysostaphin SH3b domain in complex with a pentaglycine peptide representing the peptidoglycan cross-bridge. The structure identifies a groove between β1 and β2 strands as the pentaglycine binding site. The structure suggests that pentaglycine specificity of the SH3b arises partially directly by steric exclusion of Cβ atoms in the ligand and partially indirectly due to the selection of main chain conformations that are easily accessible for glycine, but not other amino acid residues. We have revealed further interactions of SH3b with the stem peptides with the support of bioinformatics tools. Based on the structural data we have attempted engineering of the domain specificity and have investigated the relevance of the introduced substitutions on the domain binding and specificity, also in the contexts of the mature lysostaphin and of its bacteriolytic activity.
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