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TitleStructure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein.
Journal, issue, pagesStructure, Year 2025
Publish dateMar 24, 2025
AuthorsJames L Kizziah / Amarshi Mukherjee / Laura K Parker / Terje Dokland /
PubMed AbstractThe Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, ...The Staphylococcus aureus pathogenicity islands (SaPIs), including SaPI1, are a type of mobile genetic elements (MGEs) that are mobilized at high frequency by "helper" bacteriophages, such as 80α, leading to packaging of the SaPI genomes into virions made from helper-encoded structural proteins. 80α and SaPI1 virions consist of an icosahedral head connected via a portal vertex to a long, non-contractile tail. A connector or "neck" forms the interface between the tail and the head. Here, we have determined the high-resolution structure of the neck section of SaPI1 virions, including the dodecameric portal and head-tail-connector proteins, and the hexameric head-tail joining, tail terminator and major tail proteins. We also resolved the DNA, the tail completion protein (TCP), and the tape measure protein (TMP) inside the tail, features that have not previously been observed at high resolution. Our study provides insights into the assembly and infection process in this important group of MGEs.
External linksStructure / PubMed:40174589
MethodsEM (single particle)
Resolution3.14 Å
Structure data

48618

9mu3

EMDB-48618, PDB-9mu3:
SaPI1 neck structure
Method: EM (single particle) / Resolution: 3.14 Å

Source
  • staphylococcus phage 80alpha (virus)
KeywordsVIRUS LIKE PARTICLE / sapi / capsid / tail / phage

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