8TVA

Outer Mat-T4P complex

これはPDB形式変換不可エントリーです。

8TVA の概要

• エントリーDOI: 10.2210/pdb8tva/pdb
• EMDBエントリー: 41442 41443 41634 41635
• 分子名称: Maturation protein, Fimbrial protein (3 entities in total)
• 機能のキーワード: acinetobacter, ssrna phage virus, t4p, virus
• 由来する生物種: Acinetobacter phage AP205; 詳細
• タンパク質・核酸の鎖数: 41
• 化学式量合計: 350474.35

構造登録者

Meng, R.,Xing, Z.,Thongchol, J.,Zhang, J. (登録日: 2023-08-17, 公開日: 2024-03-06, 最終更新日: 2024-10-09)

主引用文献

Meng, R.,Xing, Z.,Chang, J.Y.,Yu, Z.,Thongchol, J.,Xiao, W.,Wang, Y.,Chamakura, K.,Zeng, Z.,Wang, F.,Young, R.,Zeng, L.,Zhang, J.
Structural basis of Acinetobacter type IV pili targeting by an RNA virus.
Nat Commun, 15:2746-2746, 2024

PubMed Abstract: Acinetobacters pose a significant threat to human health, especially those with weakened immune systems. Type IV pili of acinetobacters play crucial roles in virulence and antibiotic resistance. Single-stranded RNA bacteriophages target the bacterial retractile pili, including type IV. Our study delves into the interaction between Acinetobacter phage AP205 and type IV pili. Using cryo-electron microscopy, we solve structures of the AP205 virion with an asymmetric dimer of maturation proteins, the native Acinetobacter type IV pili bearing a distinct post-translational pilin cleavage, and the pili-bound AP205 showing its maturation proteins adapted to pilin modifications, allowing each phage to bind to one or two pili. Leveraging these results, we develop a 20-kilodalton AP205-derived protein scaffold targeting type IV pili in situ, with potential for research and diagnostics.

PubMed: 38553443
DOI: 10.1038/s41467-024-47119-5

実験手法

ELECTRON MICROSCOPY (8.55 Å)