8TOC

Acinetobacter phage AP205

This is a non-PDB format compatible entry.

Summary for 8TOC

• Entry DOI: 10.2210/pdb8toc/pdb
• EMDB information: 41442 41443 41634 41635
• Descriptor: RNA (4269-MER), Maturation protein, Coat protein (3 entities in total)
• Functional Keywords: acinetobacter, ssrna phage virus, virus, virus-rna complex, virus/rna
• Biological source: Bacteria abnormis; More
• Total number of polymer chains: 181
• Total formula weight: 3950698.36

Authors

Meng, R.,Xing, Z.,Chang, J.,Zhang, J. (deposition date: 2023-08-03, release date: 2024-03-06, Last modification date: 2024-04-10)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.11 Å)