8B3P

CryoEM structure of the round tip (proteins pVII/pVIII/pIX) from the f1 filamentous bacteriophage

これはPDB形式変換不可エントリーです。

8B3P の概要

• エントリーDOI: 10.2210/pdb8b3p/pdb
• EMDBエントリー: 15832
• 分子名称: Tail virion protein G7P, Tail virion protein G9P, Capsid protein G8P (3 entities in total)
• 機能のキーワード: viral proteins, assembly, virus
• 由来する生物種: Enterobacteria phage f1; 詳細
• タンパク質・核酸の鎖数: 55
• 化学式量合計: 270833.37

構造登録者

Conners, R.,McLaren, M.,Gold, V.A.M. (登録日: 2022-09-16, 公開日: 2023-05-24, 最終更新日: 2024-07-24)

主引用文献

Conners, R.,Leon-Quezada, R.I.,McLaren, M.,Bennett, N.J.,Daum, B.,Rakonjac, J.,Gold, V.A.M.
Cryo-electron microscopy of the f1 filamentous phage reveals insights into viral infection and assembly.
Nat Commun, 14:2724-2724, 2023

PubMed Abstract: Phages are viruses that infect bacteria and dominate every ecosystem on our planet. As well as impacting microbial ecology, physiology and evolution, phages are exploited as tools in molecular biology and biotechnology. This is particularly true for the Ff (f1, fd or M13) phages, which represent a widely distributed group of filamentous viruses. Over nearly five decades, Ffs have seen an extraordinary range of applications, yet the complete structure of the phage capsid and consequently the mechanisms of infection and assembly remain largely mysterious. In this work, we use cryo-electron microscopy and a highly efficient system for production of short Ff-derived nanorods to determine a structure of a filamentous virus including the tips. We show that structure combined with mutagenesis can identify phage domains that are important in bacterial attack and for release of new progeny, allowing new models to be proposed for the phage lifecycle.

PubMed: 37169795
DOI: 10.1038/s41467-023-37915-w

実験手法

ELECTRON MICROSCOPY (2.81 Å)