| Literature DB >> 28404851 |
Jingwei Xu1, Ye Xiang2.
Abstract
The bacteriophage ϕ29 infects Gram-positive Bacillus subtilis with a short noncontractile tail. Recent studies showed that the ϕ29 tail protein gp9 forms a hexameric tube with six long loops of membrane-active peptides blocking in the tube at the distal end of the tail. The long loops exit on genome release and form a membrane pore for passage of the genome. The membrane penetration mechanism of the ϕ29 tail might be common among tailed bacteriophages.Entities:
Keywords: bacteriophages; cryoEM; crystal structure; gp9; membrane penetration; membrane-active peptide; short noncontractile tail; tail knob; ϕ29
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Year: 2017 PMID: 28404851 PMCID: PMC5469264 DOI: 10.1128/JVI.00162-17
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103