8UEJ

ssRNA phage PhiCb5 virion

This is a non-PDB format compatible entry.

Summary for 8UEJ

• Entry DOI: 10.2210/pdb8uej/pdb
• EMDB information: 42163
• Descriptor: Coat protein, Maturation protein, CALCIUM ION (3 entities in total)
• Functional Keywords: ssrna phage, virus
• Biological source: Caulobacter phage phiCb5; More
• Total number of polymer chains: 179
• Total formula weight: 2453002.36

Authors

Wang, Y.,Zhang, J. (deposition date: 2023-10-01, release date: 2024-05-15, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.7 Å)