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| Title | The architecture and stabilisation of flagellotropic tailed bacteriophages. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 11, Issue 1, Page 3748, Year 2020 |
| Publish date | Jul 27, 2020 |
 Authors | Joshua M Hardy / Rhys A Dunstan / Rhys Grinter / Matthew J Belousoff / Jiawei Wang / Derek Pickard / Hariprasad Venugopal / Gordon Dougan / Trevor Lithgow / Fasséli Coulibaly /   |
| PubMed Abstract | Flagellotropic bacteriophages engage flagella to reach the bacterial surface as an effective means to increase the capture radius for predation. Structural details of these viruses are of great ...Flagellotropic bacteriophages engage flagella to reach the bacterial surface as an effective means to increase the capture radius for predation. Structural details of these viruses are of great interest given the substantial drag forces and torques they face when moving down the spinning flagellum. We show that the main capsid and auxiliary proteins form two nested chainmails that ensure the integrity of the bacteriophage head. Core stabilising structures are conserved in herpesviruses suggesting their ancestral origin. The structure of the tail also reveals a robust yet pliable assembly. Hexameric rings of the tail-tube protein are braced by the N-terminus and a β-hairpin loop, and interconnected along the tail by the splayed β-hairpins. By contrast, we show that the β-hairpin has an inhibitory role in the tail-tube precursor, preventing uncontrolled self-assembly. Dyads of acidic residues inside the tail-tube present regularly-spaced motifs well suited to DNA translocation into bacteria through the tail. |
 External links | Nat Commun / PubMed:32719311 / PubMed Central |
| Methods | EM (single particle) / EM (helical sym.) / X-ray diffraction |
| Resolution | 2.6 - 3.8 Å |
| Structure data | EMDB-22182, PDB-6xgq: EMDB-22183, PDB-6xgr:  PDB-6xgp: |
| Chemicals |  ChemComp-HOH: |
| Source |
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 Keywords |  VIRAL PROTEIN / capsid protein / VIRUS / Bacteriophage capsid / Bacteriophage tail / helical assembly |
