ArticleViruses2015
Structure of the Receptor-Binding Carboxy-Terminal Domain of the Bacteriophage T5 L-Shaped Tail Fibre with and without Its Intra-Molecular Chaperone.
Article in Viruses, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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44 citing papers in PubMed.
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- Structure of a Brochothrix thermosphacta bacteriophage reveals cell wall adsorption mechanism in Gram-positive infecting siphophages.Nature communications · 2026Article
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- Characterization and comparative genome analysis of a new Tequintavirus isolated on Salmonella enterica serotype Tennessee.BMC research notes · 2025Article
- KlebPhaCol: a community-driven resource for Klebsiella research identified a novel phage family.Nucleic acids research · 2025Article
- The host range of generalist and specialist phages in capsule-diverse Klebsiella hosts is driven by the evolvability of receptor-binding proteins.PLoS biology · 2025Article
- Characterization of strictly lytic phages infectingMicrobiology spectrum · 2025Article
- Interplay Between Bacterial Extracellular Vesicles and Phages: Receptors, Mechanisms, and Implications.Viruses · 2025Review
- Phage Host Range Expansion Through Directed Evolution on Highly Phage-Resistant Strains ofInternational journal of molecular sciences · 2025Article
- Amino acid residues in the tail fiber differentiate the host specificity ofJournal of virology · 2025Article
- Completing the BASEL phage collection to unlock hidden diversity for systematic exploration of phage-host interactions.PLoS biology · 2025Article
- About proteins of a siphophage tail tip complex reverting to their pre-ejection fold after DNA ejection.Nature communications · 2025Article
- Revisiting phage tail spike architecture: evidence for undetected receptor-binding proteins inFrontiers in microbiology · 2025Article
- The TolC and Lipopolysaccharide-SpecificPHAGE (New Rochelle, N.Y.) · 2024Article
- DepoScope: Accurate phage depolymerase annotation and domain delineation using large language models.PLoS computational biology · 2024Article
- Bacteriophage Receptor Recognition and Nucleic Acid Transfer.Sub-cellular biochemistry · 2024Review
- Bdellovibrio bacteriovorus uses chimeric fibre proteins to recognize and invade a broad range of bacterial hosts.Nature microbiology · 2024Article
- Distantly related Alteromonas bacteriophages share tail fibers exhibiting properties of transient chaperone caps.Nature communications · 2023Article
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9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacteriophage T5, a Siphovirus belonging to the order Caudovirales, has a flexible, three-fold symmetric tail, to which three L-shaped fibres are attached. These fibres recognize oligo-mannose units on the bacterial cell surface prior to infection and are composed of homotrimers of the pb1 protein. Pb1 has 1396 amino acids, of which the carboxy-terminal 133 residues form a trimeric intra-molecular chaperone that is auto-proteolyzed after correct folding. The structure of a trimer of residues 970-1263 was determined by single anomalous dispersion phasing using incorporated selenomethionine residues and refined at 2.3 Å resolution using crystals grown from native, methionine-containing, protein. The protein inhibits phage infection by competition. The phage-distal receptor-binding domain resembles a bullet, with the walls formed by partially intertwined beta-sheets, conferring stability to the structure. The fold of the domain is novel and the topology unique to the pb1 structure. A site-directed mutant (Ser1264 to Ala), in which auto-proteolysis is impeded, was also produced, crystallized and its 2.5 Å structure solved by molecular replacement. The additional chaperone domain (residues 1263-1396) consists of a central trimeric alpha-helical coiled-coil flanked by a mixed alpha-beta domain. Three long beta-hairpin tentacles, one from each chaperone monomer, extend into long curved grooves of the bullet-shaped domain. The chaperone-containing mutant did not inhibit infection by competition.
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