ArticleJournal of virology2014
Crystal structure of pb9, the distal tail protein of bacteriophage T5: a conserved structural motif among all siphophages.
Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 56 citations in OpenAlex.
- Article
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- Characterization of strictly lytic phages infectingMicrobiology spectrum · 2025Article
- Proteomic Analysis of Marine Bacteriophages: Structural Conservation, Post-Translational Modifications, and Phage-Host Interactions.Environmental microbiology · 2025Article
- About proteins of a siphophage tail tip complex reverting to their pre-ejection fold after DNA ejection.Nature communications · 2025Article
- About bacteriophage tail terminator and tail completion proteins: structure of the proximal extremity of siphophage T5 tail.Journal of virology · 2025Article
- Isolation of phages infecting the zoonotic pathogenbioRxiv : the preprint server for biology · 2025Article
- Article
- Active prophages in coral-associated Halomonas capable of lateral transduction.The ISME journal · 2024Article
- Structure and proposed DNA delivery mechanism of a marine roseophage.Nature communications · 2023Article
- Structural basis of bacteriophage T5 infection trigger andScience advances · 2023Article
- Phage Adsorption to Gram-Positive Bacteria.Viruses · 2023Review
- Exploring Structural Diversity among Adhesion Devices Encoded by Lactococcal P335 Phages with AlphaFold2.Microorganisms · 2022Article
- Expansion of the Plaquing Host Range and Improvement of the Absorption Rate of a T5-like Salmonella Phage by Altering the Long Tail Fibers.Applied and environmental microbiology · 2022Article
- A structural discovery journey of streptococcal phages adhesion devices by AlphaFold2.Frontiers in molecular biosciences · 2022Article
- Article
- BtuB-Dependent Infection of the T5-likeViruses · 2021Article
- Structure and Topology Prediction of Phage Adhesion Devices Using AlphaFold2: The Case of TwoMicroorganisms · 2021Article
- A LyticFrontiers in cellular and infection microbiology · 2021Article
Corrections and comments
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Authors and funding
8 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tail of Caudovirales bacteriophages serves as an adsorption device, a host cell wall-perforating machine, and a genome delivery pathway. In Siphoviridae, the assembly of the long and flexible tail is a highly cooperative and regulated process that is initiated from the proteins forming the distal tail tip complex. In Gram-positive-bacterium-infecting siphophages, the distal tail (Dit) protein has been structurally characterized and is proposed to represent a baseplate hub docking structure. It is organized as a hexameric ring that connects the tail tube and the adsorption device. In this study, we report the characterization of pb9, a tail tip protein of Escherichia coli bacteriophage T5. By immunolocalization, we show that pb9 is located in the upper part of the cone of the T5 tail tip, at the end of the tail tube. The crystal structure of pb9 reveals a two-domain protein. Domain A exhibits remarkable structural similarity with the N-terminal domain of known Dit proteins, while domain B adopts an oligosaccharide/oligonucleotide-binding fold (OB-fold) that is not shared by these proteins. We thus propose that pb9 is the Dit protein of T5, making it the first Dit protein described for a Gram-negative-bacterium-infecting siphophage. Multiple sequence alignments suggest that pb9 is a paradigm for a large family of Dit proteins of siphophages infecting mostly Gram-negative hosts. The modular structure of the Dit protein maintains the basic building block that would be conserved among all siphophages, combining it with a more divergent domain that might serve specific host adhesion properties.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.