Summary information and primary citation
- PDB-id
-
8qem;
DSSR-derived features in text and
JSON formats
- Class
- virus
- Method
- cryo-EM (3.96 Å)
- Summary
- Neck channel of phage 812 after tail contraction
(c1)
- Reference
-
Cienikova Z, Novacek J, Siborova M, Popelarova B, Fuzik
T, Botka T, Benesik M, Bardy P, Pantucek R, Plevka P
(2026): "Genome
anchoring, retention, and release by neck proteins of
Staphylococcus phage 812." Commun Biol. doi:
10.1038/s42003-025-09477-8.
- Abstract
- The virion of Staphylococcus phage 812 is formed by a
capsid and a contractile tail joined together by neck
proteins. The neck proteins are crucial for virion
assembly, DNA packaging, and the regulation of genome
release, but their functions are not completely understood.
Here, we show that the neck of phage 812 consists of
portal, adaptor, stopper, tail terminator, and two types of
decoration proteins. A dodecameric DNA-binding site at the
surface of the portal complex anchors the phage genome
inside the capsid. The adaptor complex induces a local
B-to-A form transition of the DNA in the neck channel that
could slow or pause genome translocation during ejection.
The central channel of a stopper complex that is not
attached to the tail terminator complex is closed by gating
loops. In contrast, in the phage 812 virion, the gating
loops are in an open conformation, and the DNA extends into
the tail. The structure of neck proteins is not affected by
tail sheath contraction. Therefore, the expulsion of tail
tape measure proteins triggers the genome release.
