9MKB

Structure of the bacteriophage T4 portal-neck-tail complex

これはPDB形式変換不可エントリーです。

9MKB の概要

• エントリーDOI: 10.2210/pdb9mkb/pdb
• EMDBエントリー: 48324
• 分子名称: gp14, neck protein, Hoc, highly immunogenic outer capsid protein, Soc, small outer capsid protein, ... (32 entities in total)
• 機能のキーワード: bacteriophage t4, portal vertex, phage neck, phage tail, contractile sheath, tail tube, baseplate, virus, viral protein
• 由来する生物種: Escherichia phage T4; 詳細
• タンパク質・核酸の鎖数: 541
• 化学式量合計: 24141063.30

構造登録者

Fokine, A.,Zhu, J.,Klose, T.,Vago, F.,Arnaud, C.,Wang, Z.,Khare, B.,Rossmann, M.G.,Chen, Z.,Sun, L.,Fang, Q.,Kuhn, R.,Rao, V.B. (登録日: 2024-12-17, 公開日: 2025-12-24, 最終更新日: 2026-07-08)

主引用文献

Fokine, A.,Zhu, J.,Klose, T.,Vago, F.,Arnaud, C.A.,Wang, Z.,Khare, B.,Rossmann, M.G.,Chen, Z.,Sun, L.,Fang, Q.,Kuhn, R.J.,Rao, V.B.
In situ structures of the portal-neck-tail complex of bacteriophage T4 inform a viral genome positioning mechanism.
Nat Commun, 17:-, 2026

PubMed Abstract: The post-genome packaging mechanisms that govern the assembly of an infectious virion are poorly understood in bacteriophages and other viruses. Here, our near-atomic resolution cryo-EM structural analyses uncovered an assembly- and conformation-driven genome positioning mechanism in the tailed bacteriophage T4. We show that following headful packaging, which generates a pressurized head, a global conformational change occurs in the portal structure, probably triggering packaging termination and ejection of the packaging motor. Our high-resolution structures of the neck of the virion further show that the neck undergoes conformational changes upon docking of a pre-assembled tail onto the sealed neck, which then opens a genome-gate. Driven by the pressure of the packaged DNA, the genome travels through open neck channels, binds and compresses the resident tape-measure protein, and halts at the bottom of the second topmost disk of the tail tube. Pressure-suspended within the virion's innermost tunnel and secured by a baseplate plug, the genome remains poised to flow through the tunnel into a host cell upon receiving the host receptor recognition signal.

PubMed: 41720772
DOI: 10.1038/s41467-026-69106-8

実験手法

ELECTRON MICROSCOPY (3.8 Å)