6V1I

Cryo-EM reconstruction of the thermophilic bacteriophage P74-26 small terminase- symmetric

6V1I の概要

• エントリーDOI: 10.2210/pdb6v1i/pdb
• EMDBエントリー: 21012
• 分子名称: Small terminase protein (1 entity in total)
• 機能のキーワード: small terminase, bacteriophage, helix-turn-helix, motor, viral protein
• 由来する生物種: Thermus virus P74-26
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 171727.98

構造登録者

Hayes, J.A.,Hilbert, B.J.,Gaubitz, C.,Stone, N.P.,Kelch, B.A. (登録日: 2019-11-20, 公開日: 2020-02-12, 最終更新日: 2024-03-06)

主引用文献

Hayes, J.A.,Hilbert, B.J.,Gaubitz, C.,Stone, N.P.,Kelch, B.A.
A thermophilic phage uses a small terminase protein with a fixed helix-turn-helix geometry.
J.Biol.Chem., 295:3783-3793, 2020

PubMed Abstract: Tailed bacteriophages use a DNA-packaging motor to encapsulate their genome during viral particle assembly. The small terminase (TerS) component of this DNA-packaging machinery acts as a molecular matchmaker that recognizes both the viral genome and the main motor component, the large terminase (TerL). However, how TerS binds DNA and the TerL protein remains unclear. Here we identified gp83 of the thermophilic bacteriophage P74-26 as the TerS protein. We found that TerS oligomerizes into a nonamer that binds DNA, stimulates TerL ATPase activity, and inhibits TerL nuclease activity. A cryo-EM structure of TerS revealed that it forms a ring with a wide central pore and radially arrayed helix-turn-helix domains. The structure further showed that these helix-turn-helix domains, which are thought to bind DNA by wrapping the double helix around the ring, are rigidly held in an orientation distinct from that seen in other TerS proteins. This rigid arrangement of the putative DNA-binding domain imposed strong constraints on how TerS can bind DNA. Finally, the TerS structure lacked the conserved C-terminal β-barrel domain used by other TerS proteins for binding TerL. This suggests that a well-ordered C-terminal β-barrel domain is not required for TerS to carry out its matchmaking function. Our work highlights a thermophilic system for studying the role of small terminase proteins in viral maturation and presents the structure of TerS, revealing key differences between this thermophilic phage and its mesophilic counterparts.

PubMed: 32014998
DOI: 10.1074/jbc.RA119.012224

実験手法

ELECTRON MICROSCOPY (3.8 Å)