8B3P

CryoEM structure of the round tip (proteins pVII/pVIII/pIX) from the f1 filamentous bacteriophage

This is a non-PDB format compatible entry.

Summary for 8B3P

• Entry DOI: 10.2210/pdb8b3p/pdb
• EMDB information: 15832
• Descriptor: Tail virion protein G7P, Tail virion protein G9P, Capsid protein G8P (3 entities in total)
• Functional Keywords: viral proteins, assembly, virus
• Biological source: Enterobacteria phage f1; More
• Total number of polymer chains: 55
• Total formula weight: 270833.37

Authors

Conners, R.,McLaren, M.,Gold, V.A.M. (deposition date: 2022-09-16, release date: 2023-05-24, Last modification date: 2024-07-24)

Primary citation

Conners, R.,Leon-Quezada, R.I.,McLaren, M.,Bennett, N.J.,Daum, B.,Rakonjac, J.,Gold, V.A.M.
Cryo-electron microscopy of the f1 filamentous phage reveals insights into viral infection and assembly.
Nat Commun, 14:2724-2724, 2023

PubMed Abstract: Phages are viruses that infect bacteria and dominate every ecosystem on our planet. As well as impacting microbial ecology, physiology and evolution, phages are exploited as tools in molecular biology and biotechnology. This is particularly true for the Ff (f1, fd or M13) phages, which represent a widely distributed group of filamentous viruses. Over nearly five decades, Ffs have seen an extraordinary range of applications, yet the complete structure of the phage capsid and consequently the mechanisms of infection and assembly remain largely mysterious. In this work, we use cryo-electron microscopy and a highly efficient system for production of short Ff-derived nanorods to determine a structure of a filamentous virus including the tips. We show that structure combined with mutagenesis can identify phage domains that are important in bacterial attack and for release of new progeny, allowing new models to be proposed for the phage lifecycle.

PubMed: 37169795
DOI: 10.1038/s41467-023-37915-w

Experimental method

ELECTRON MICROSCOPY (2.81 Å)