7Z4W

gp6/gp15/gp16 connector complex of bacteriophage SPP1

7Z4W の概要

• エントリーDOI: 10.2210/pdb7z4w/pdb
• EMDBエントリー: 14509
• 分子名称: Portal protein, Head completion protein gp15, Head completion protein gp16, ... (4 entities in total)
• 機能のキーワード: bacteriophage, spp1, portal protein, head completion proteins, connector complex, dna channel, viral protein
• 由来する生物種: Bacillus subtilis; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 903566.09

構造登録者

Orlov, I.,Roche, S.,Tavares, P.,Orlova, E.V. (登録日: 2022-03-05, 公開日: 2022-11-30, 最終更新日: 2024-07-17)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (2.7 Å)