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TitleCryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 7283, Year 2022
Publish dateNov 26, 2022
AuthorsIgor Orlov / Stéphane Roche / Sandrine Brasilès / Natalya Lukoyanova / Marie-Christine Vaney / Paulo Tavares / Elena V Orlova /
PubMed AbstractNumerous viruses package their dsDNA genome into preformed capsids through a portal gatekeeper that is subsequently closed. We report the structure of the DNA gatekeeper complex of bacteriophage SPP1 ...Numerous viruses package their dsDNA genome into preformed capsids through a portal gatekeeper that is subsequently closed. We report the structure of the DNA gatekeeper complex of bacteriophage SPP1 (gp6gp15gp16) in the post-DNA packaging state at 2.7 Å resolution obtained by single particle cryo-electron microscopy. Comparison of the native SPP1 complex with assembly-naïve structures of individual components uncovered the complex program of conformational changes leading to its assembly. After DNA packaging, gp15 binds via its C-terminus to the gp6 oligomer positioning gp15 subunits for oligomerization. Gp15 refolds its inner loops creating an intersubunit β-barrel that establishes different types of contacts with six gp16 subunits. Gp16 binding and oligomerization is accompanied by folding of helices that close the portal channel to keep the viral genome inside the capsid. This mechanism of assembly has broad functional and evolutionary implications for viruses of the prokaryotic tailed viruses-herpesviruses lineage.
External linksNat Commun / PubMed:36435855 / PubMed Central
MethodsEM (single particle)
Resolution2.7 Å
Structure data

14509

7z4w

EMDB-14509, PDB-7z4w:
gp6/gp15/gp16 connector complex of bacteriophage SPP1
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-HOH:
WATER / Water

Source
  • bacillus subtilis (bacteria)
KeywordsVIRAL PROTEIN / Bacteriophage / SPP1 / Portal Protein / Head completion proteins / Connector Complex / DNA Channel

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