8VJI

Cryo-EM of capsid of bacteriophage Chi

Summary for 8VJI

• Entry DOI: 10.2210/pdb8vji/pdb
• EMDB information: 43282
• Descriptor: Major capsid protein, Decorator protein D (2 entities in total)
• Functional Keywords: flagellotropic bacteriophage, siphophage, capsid, virus
• Biological source: Chivirus chi; More
• Total number of polymer chains: 14
• Total formula weight: 380524.70

Authors

Sonani, R.R.,Esteves, N.C.,Scharf, B.E.,Egelman, E.H. (deposition date: 2024-01-06, release date: 2024-10-02)

Primary citation

Sonani, R.R.,Esteves, N.C.,Scharf, B.E.,Egelman, E.H.
Cryo-EM structure of flagellotropic bacteriophage Chi.
Structure, 32:856-865.e3, 2024

PubMed Abstract: The flagellotropic bacteriophage χ (Chi) infects bacteria via the flagellar filament. Despite years of study, its structural architecture remains partly characterized. Through cryo-EM, we unveil χ's nearly complete structure, encompassing capsid, neck, tail, and tail tip. While the capsid and tail resemble phage YSD1, the neck and tail tip reveal new proteins and their arrangement. The neck shows a unique conformation of the tail tube protein, forming a socket-like structure for attachment to the neck. The tail tip comprises four proteins, including distal tail protein (DTP), two baseplate hub proteins (BH1P and BH2P), and tail tip assembly protein (TAP) exhibiting minimal organization compared to other siphophages. Deviating from the consensus in other siphophages, DTP in χ forms a trimeric assembly, reducing tail symmetry from 6-fold to 3-fold at the tip. These findings illuminate the previously unexplored structural organization of χ's neck and tail tip.

PubMed: 38614087
DOI: 10.1016/j.str.2024.03.011

Experimental method

ELECTRON MICROSCOPY (3.3 Å)