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TitleStructure of a Bacterial Virus DNA-Injection Protein Complex Reveals a Decameric Assembly with a Constricted Molecular Channel.
Journal, issue, pagesPLoS One, Vol. 11, Issue 2, Page e0149337, Year 2016
Publish dateFeb 16, 2016
AuthorsHaiyan Zhao / Jeffrey A Speir / Tsutomu Matsui / Zihan Lin / Lingfei Liang / Anna Y Lynn / Brittany Varnado / Thomas M Weiss / Liang Tang /
PubMed AbstractThe multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we ...The multi-layered cell envelope structure of Gram-negative bacteria represents significant physical and chemical barriers for short-tailed phages to inject phage DNA into the host cytoplasm. Here we show that a DNA-injection protein of bacteriophage Sf6, gp12, forms a 465-kDa, decameric assembly in vitro. The electron microscopic structure of the gp12 assembly shows a ~150-Å, mushroom-like architecture consisting of a crown domain and a tube-like domain, which embraces a 25-Å-wide channel that could precisely accommodate dsDNA. The constricted channel suggests that gp12 mediates rapid, uni-directional injection of phage DNA into host cells by providing a molecular conduit for DNA translocation. The assembly exhibits a 10-fold symmetry, which may be a common feature among DNA-injection proteins of P22-like phages and may suggest a symmetry mismatch with respect to the 6-fold symmetric phage tail. The gp12 monomer is highly flexible in solution, supporting a mechanism for translocation of the protein through the conduit of the phage tail toward the host cell envelope, where it assembles into a DNA-injection device.
External linksPLoS One / PubMed:26882199 / PubMed Central
MethodsEM (single particle)
Resolution11.0 Å
Structure data

EMDB-6330:
3D structure of the decameric assembly of the DNA-injection protein gp12 from bacteriophage Sf6
Method: EM (single particle) / Resolution: 11.0 Å

Source
  • Bacillus phage SF6 (virus)

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