ArticleScientific reports2019
Structure and tailspike glycosidase machinery of ORF212 from E. coli O157:H7 phage CBA120 (TSP3).
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 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
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- TSPDB: a curated resource of tailspike proteins with potential applications in phage research.Frontiers in big data · 2024Article
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- Complete Genome Sequence of Klebsiella pneumoniae Bacteriophage KpS110, Encoding Five Tail-Associated Proteins with Putative Polysaccharide Depolymerase Domains.Microbiology resource announcements · 2023Article
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- Structure of Escherichia coli O157:H7 bacteriophage CBA120 tailspike protein 4 baseplate anchor and tailspike assembly domains (TSP4-N).Scientific reports · 2022Article
- Genomic Diversity of Bacteriophages Infecting the GenusViruses · 2022Article
- Characterization and Functional Studies of a Novel Depolymerase Against K19-TypeFrontiers in microbiology · 2022Article
- Computational models in the service of X-ray and cryo-electron microscopy structure determination.Proteins · 2021Article
- Characterization of a novel phage depolymerase specific to Escherichia coli O157:H7 and biofilm control on abiotic surfaces.Journal of microbiology (Seoul, Korea) · 2021Article
- Novel Phage-Derived Depolymerase with Activity againstMicroorganisms · 2021Article
- Reprogramming bacteriophage host range: design principles and strategies for engineering receptor binding proteins.Current opinion in biotechnology · 2021Review
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Bacteriophage tailspike proteins mediate virion absorption through reversible primary receptor binding, followed by lipopolysaccharide or exopolysaccharide degradation. The Escherichia coli O157:H7 bacteriophage CBA120 genome encodes four distinct tailspike proteins, annotated as ORFs 210 through 213. Previously, we reported the crystal structure of ORF210 (TSP1). Here we describe the crystal structure of ORF212 (TSP3) determined at 1.85 Å resolution. As observed with other tailspike proteins, TSP3 assembles into a trimer. Each subunit of TSP3 has an N-terminal head domain that is structurally similar to that of TSP1, consistent with their high amino acid sequence identity. In contrast, despite sharing a β-helix fold, the overall structure of the C-terminal catalytic domain of TSP3 is quite different when compared to TSP1. The TSP3 structure suggests that the glycosidase active site resides in a cleft at the interface between two adjacent subunits where three acidic residues, Glu362 and Asp383 on one subunit, and Asp426 on a second subunit, are located in close proximity. Comparing the glycosidase activity of wild-type TSP3 to various point mutants revealed that catalysis requires the carboxyl groups of Glu362 and Asp426, and not of Asp383, confirming the enzyme employs two carboxyl groups to degrade lippopolysaccharide using an acid/base mechanism.
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