{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Linares R"],"funding":["Agence Nationale de la Recherche (ANR)","Agence Nationale de la Recherche"],"pagination":["e0137624"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11784142"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["99(1)"],"pubmed_abstract":["Bacteriophages are viruses infecting bacteria. The vast majority of them bear a tail, allowing host recognition, cell wall perforation, and DNA injection into the host cytoplasm. Using electron cryo-microscopy (cryo-EM) and single particle analysis, we determined the organization of the tail proximal extremity of siphophage T5 that possesses a long flexible tail and solved the structure of its tail terminator protein p142 (TrP<sub>142</sub>). It allowed us to confirm the common evolutionary origin between T5 TrP<sub>p142</sub> and other known or putative TrPs from siphophages, myophages, and bacterial tail-like machines, despite very poor sequence conservation. By also determining the structure of the T5 tail proximal extremity after interaction with T5 bacterial receptor FhuA, we showed t"],"journal":["Journal of virology"],"pubmed_title":["About bacteriophage tail terminator and tail completion proteins: structure of the proximal extremity of siphophage T5 tail."],"pmcid":["PMC11784142"],"funding_grant_id":["Projet ANR-20-CE11-0023"],"pubmed_authors":["Breyton C","Linares R"],"additional_accession":[]},"is_claimable":false,"name":"About bacteriophage tail terminator and tail completion proteins: structure of the proximal extremity of siphophage T5 tail.","description":"Bacteriophages are viruses infecting bacteria. The vast majority of them bear a tail, allowing host recognition, cell wall perforation, and DNA injection into the host cytoplasm. Using electron cryo-microscopy (cryo-EM) and single particle analysis, we determined the organization of the tail proximal extremity of siphophage T5 that possesses a long flexible tail and solved the structure of its tail terminator protein p142 (TrP<sub>142</sub>). It allowed us to confirm the common evolutionary origin between T5 TrP<sub>p142</sub> and other known or putative TrPs from siphophages, myophages, and bacterial tail-like machines, despite very poor sequence conservation. By also determining the structure of the T5 tail proximal extremity after interaction with T5 bacterial receptor FhuA, we showed t","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-02T01:51:31.506Z","creation":"2025-04-07T04:19:34.55Z"},"accession":"S-EPMC11784142","cross_references":{"pubmed":["39714170"],"doi":["10.1128/jvi.01376-24"]}}