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| Title | Electron cryo-microscopy of bacteriophage PR772 reveals the elusive vertex complex and the capsid architecture. |
|---|---|
| Journal, issue, pages | Elife, Vol. 8, Year 2019 |
| Publish date | Sep 12, 2019 |
 Authors | Hemanth Kn Reddy / Marta Carroni / Janos Hajdu / Martin Svenda /   |
| PubMed Abstract | Bacteriophage PR772, a member of the family, has a 70 nm diameter icosahedral protein capsid that encapsulates a lipid membrane, dsDNA, and various internal proteins. An icosahedrally averaged ...Bacteriophage PR772, a member of the family, has a 70 nm diameter icosahedral protein capsid that encapsulates a lipid membrane, dsDNA, and various internal proteins. An icosahedrally averaged CryoEM reconstruction of the wild-type virion and a localized reconstruction of the vertex region reveal the composition and the structure of the vertex complex along with new protein conformations that play a vital role in maintaining the capsid architecture of the virion. The overall resolution of the virion is 2.75 Å, while the resolution of the protein capsid is 2.3 Å. The conventional penta-symmetron formed by the capsomeres is replaced by a large vertex complex in the pseudo T = 25 capsid. All the vertices contain the host-recognition protein, P5; two of these vertices show the presence of the receptor-binding protein, P2. The 3D structure of the vertex complex shows interactions with the viral membrane, indicating a possible mechanism for viral infection. |
 External links | Elife / PubMed:31513011 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 2.75 - 10.0 Å |
| Structure data |  EMDB-10237:  EMDB-10238: EMDB-4461, PDB-6q5u:  EMDB-4462: |
| Source |
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 Keywords |  VIRUS / Phage / Tectiviridae / Membrane / double-barrel / helix turn helix / helix with a kink / beta-propeller / heteropentamer / penton |
enterobacteria phage pr772 (virus)
