EMD-41666

Single-particle
3.0 Å
EMD-41666 Deposition: 20/08/2023
Map released: 06/03/2024
Last modified: 09/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-41666

Acinetobacter phage AP205 T=3 VLP

EMD-41666

Single-particle
3.0 Å
EMD-41666 Deposition: 20/08/2023
Map released: 06/03/2024
Last modified: 09/10/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Acinetobacter phage AP205
Sample: Acinetobacter phage AP205
Fitted models: 8twc (Avg. Q-score: 0.46)

Deposition Authors: Meng R , Xing Z , Zhang J , Zhang J
Structural basis of Acinetobacter type IV pili targeting by an RNA virus.
Meng R , Xing Z , Chang JY, Yu Z, Thongchol J , Xiao W, Wang Y , Chamakura K , Zeng Z, Wang F , Young R , Zeng L , Zhang J
(2024) Nat Commun , 15 , 2746 - 2746
PUBMED: 38553443
DOI: doi:10.1038/s41467-024-47119-5
ISSN: 2041-1723
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.