8UEJ

ssRNA phage PhiCb5 virion

これはPDB形式変換不可エントリーです。

8UEJ の概要

• エントリーDOI: 10.2210/pdb8uej/pdb
• EMDBエントリー: 42163
• 分子名称: Coat protein, Maturation protein, CALCIUM ION (3 entities in total)
• 機能のキーワード: ssrna phage, virus
• 由来する生物種: Caulobacter phage phiCb5; 詳細
• タンパク質・核酸の鎖数: 179
• 化学式量合計: 2453002.36

構造登録者

Wang, Y.,Zhang, J. (登録日: 2023-10-01, 公開日: 2024-05-15, 最終更新日: 2024-05-22)

主引用文献

Wang, Y.,Theodore, M.,Xing, Z.,Narsaria, U.,Yu, Z.,Zeng, L.,Zhang, J.
Structural mechanisms of Tad pilus assembly and its interaction with an RNA virus.
Sci Adv, 10:eadl4450-eadl4450, 2024

PubMed Abstract: Tad (tight adherence) pili, part of the type IV pili family, are crucial for mechanosensing, surface adherence, bacteriophage (phage) adsorption, and cell-cycle regulation. Unlike other type IV pilins, Tad pilins lack the typical globular β sheet domain responsible for pilus assembly and phage binding. The mechanisms of Tad pilus assembly and its interaction with phage ΦCb5 have been elusive. Using cryo-electron microscopy, we unveiled the Tad pilus assembly mechanism, featuring a unique network of hydrogen bonds at its core. We then identified the Tad pilus binding to the ΦCb5 maturation protein (Mat) through its β region. Notably, the amino terminus of ΦCb5 Mat is exposed outside the capsid and phage/pilus interface, enabling the attachment of fluorescent and affinity tags. These engineered ΦCb5 virions can be efficiently assembled and purified in , maintaining infectivity against , which presents promising applications, including RNA delivery and phage display.

PubMed: 38701202
DOI: 10.1126/sciadv.adl4450

実験手法

ELECTRON MICROSCOPY (2.7 Å)