7Z4W

gp6/gp15/gp16 connector complex of bacteriophage SPP1

Summary for 7Z4W

• Entry DOI: 10.2210/pdb7z4w/pdb
• EMDB information: 14509
• Descriptor: Portal protein, Head completion protein gp15, Head completion protein gp16, ... (4 entities in total)
• Functional Keywords: bacteriophage, spp1, portal protein, head completion proteins, connector complex, dna channel, viral protein
• Biological source: Bacillus subtilis; More
• Total number of polymer chains: 30
• Total formula weight: 903566.09

Authors

Orlov, I.,Roche, S.,Tavares, P.,Orlova, E.V. (deposition date: 2022-03-05, release date: 2022-11-30, Last modification date: 2024-07-17)

Primary citation

Orlov, I.,Roche, S.,Brasiles, S.,Lukoyanova, N.,Vaney, M.C.,Tavares, P.,Orlova, E.V.
CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper.
Nat Commun, 13:7283-7283, 2022

PubMed Abstract: 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.

PubMed: 36435855
DOI: 10.1038/s41467-022-34999-8

Experimental method

ELECTRON MICROSCOPY (2.7 Å)