4EO2
Structure of the bacteriophage C1 tail knob protein, gp12
Summary for 4EO2
| Entry DOI | 10.2210/pdb4eo2/pdb |
| Related | 4EP0 |
| Descriptor | Major tail protein (1 entity in total) |
| Functional Keywords | structural protein, viral protein |
| Biological source | Streptococcus phage C1 |
| Total number of polymer chains | 6 |
| Total formula weight | 400930.78 |
| Authors | Aksyuk, A.A.,Rossmann, M.G. (deposition date: 2012-04-13, release date: 2012-08-22, Last modification date: 2024-02-28) |
| Primary citation | Aksyuk, A.A.,Bowman, V.D.,Kaufmann, B.,Fields, C.,Klose, T.,Holdaway, H.A.,Fischetti, V.A.,Rossmann, M.G. Structural investigations of a Podoviridae streptococcus phage C1, implications for the mechanism of viral entry. Proc.Natl.Acad.Sci.USA, 109:14001-14006, 2012 Cited by PubMed Abstract: The Podoviridae phage C1 was one of the earliest isolated bacteriophages and the first virus documented to be active against streptococci. The icosahedral and asymmetric reconstructions of the virus were calculated using cryo-electron microscopy. The capsid protein has an HK97 fold arranged into a T = 4 icosahedral lattice. The C1 tail is terminated with a ϕ29-like knob, surrounded by a skirt of twelve long appendages with novel morphology. Several C1 structural proteins have been identified, including a candidate for an appendage. The crystal structure of the knob has an N-terminal domain with a fold observed previously in tube forming proteins of Siphoviridae and Myoviridae phages. The structure of C1 suggests the mechanisms by which the virus digests the cell wall and ejects its genome. Although there is little sequence similarity to other phages, conservation of the structural proteins demonstrates a common origin of the head and tail, but more recent evolution of the appendages. PubMed: 22891295DOI: 10.1073/pnas.1207730109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.007 Å) |
Structure validation
Download full validation report
