ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure of the receptor-binding carboxy-terminal domain of bacteriophage T7 tail fibers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.
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85 citing papers in PubMed.
- Insights into Genome Ejection by a Therapeutic phiKMV-like Bacteriophage.Journal of molecular biology · 2026Article
- Isolation and characterization of a novel Schitoviridae phage VipHU7 that infects Vibrio parahaemolyticus.Archives of virology · 2026Article
- Development and clinical validation of a CRISPR/Cas9-engineered reporter phage cocktail for rapid detection ofMicrobiology spectrum · 2026Article
- Phage therapy: from basic biology to clinical application.Nature reviews. Microbiology · 2026Review
- Large-Scale Structural Dynamics in the Tail Fiber Modulate the Infective Transition of the T7 Bacteriophage.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- High-resolution phage-host assignment through key proteins using large language models.Nature communications · 2026Article
- From structure to design: experimental and AI-driven approaches in receptor-binding protein engineering for reprogramming phage host range.Archives of microbiology · 2026Review
- Novel Autographivirales phages Kiwi, Nika and Pie targeting Klebsiella pneumoniae K14: Isolation, characterisation, genome analysis and study of the bacterial polysaccharide degradation.Archives of virology · 2026Article
- Bentonite-Based Functional Nanoclay Enhances Bacteriophage Therapy against Enteric Infections via Toxin Adsorption and Microbiome Recovery.Biomaterials research · 2026Article
- Microgravity reshapes bacteriophage-host coevolution aboard the International Space Station.PLoS biology · 2026Article
- A synthetic cell phage cycle.Nature communications · 2025Article
- High-resolution Cryo-EM Analysis of the Therapeutic Pseudomonas Phage Pa223.Journal of molecular biology · 2025Article
- Genomic and physiochemical characterization of two lysogenic bacteriophages, ΦCP5(17) and ΦCP17(i), infecting Clostridium perfringens.Archives of virology · 2025Article
- Amino acid residues in the tail fiber differentiate the host specificity ofJournal of virology · 2025Article
- Engineering bacteriophages through deep mining of metagenomic motifs.Science advances · 2025Article
- Structure of an F-type phage tail-like bacteriocin from Listeria monocytogenes.Nature communications · 2025Article
- The structure of Shigella virus Sf14 reveals the presence of two decoration proteins and two long tail fibers.Communications biology · 2025Article
- Article
- Conformational changes in and translocation of small proteins: insights into the ejection mechanism of podophages.Journal of virology · 2025Article
- The non-nutritive sweetener rebaudioside a enhances phage infectivity.Scientific reports · 2025Article
25 more citing papers are in PubMed but not listed here.
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2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The six bacteriophage T7 tail fibers, homo-trimers of gene product 17, are thought to be responsible for the first specific, albeit reversible, attachment to Escherichia coli lipopolysaccharide. The protein trimer forms kinked fibers comprised of an amino-terminal tail-attachment domain, a slender shaft, and a carboxyl-terminal domain composed of several nodules. Previously, we expressed, purified, and crystallized a carboxyl-terminal fragment comprising residues 371-553. Here, we report the structure of this protein trimer, solved using anomalous diffraction and refined at 2 Å resolution. Amino acids 371-447 form a tapered pyramid with a triangular cross-section composed of interlocked β-sheets from each of the three chains. The triangular pyramid domain has three α-helices at its narrow end, which are connected to a carboxyl-terminal three-blade β-propeller tip domain by flexible loops. The monomers of this tip domain each contain an eight-stranded β-sandwich. The exact topology of the β-sandwich fold is novel, but similar to that of knob domains of other viral fibers and the phage Sf6 needle. Several host-range change mutants have been mapped to loops located on the top of this tip domain, suggesting that this surface of the tip domain interacts with receptors on the cell surface.
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