9MT5

Helical tail assembly of phage JohannRWettstein (Bas63)

Summary for 9MT5

• Entry DOI: 10.2210/pdb9mt5/pdb
• Related: 9MT4
• EMDB information: 48599 48600
• Descriptor: Tube protein, Structural protein (2 entities in total)
• Functional Keywords: tail, sheath, tube, phage, bas63, johannrwettstein, viral protein
• Biological source: Escherichia phage JohannRWettstein; More
• Total number of polymer chains: 2
• Total formula weight: 65119.76

Authors

Hodgkinson-Bean, J. (deposition date: 2025-01-10, release date: 2025-11-19, Last modification date: 2025-11-26)

Primary citation

Hodgkinson-Bean, J.,Ayala, R.,McJarrow-Keller, K.,Cassin, L.,Rutter, G.L.,Crowe, A.J.M.,Wolf, M.,Bostina, M.
Cryo-EM structure of bacteriophage Bas63 reveals structural conservation and diversity in the Felixounavirus genus.
Sci Adv, 11:eadx0790-eadx0790, 2025

PubMed Abstract: The BASEL phage collection was developed to provide access to diverse bacteriophages, distinct from model phages. phage JohannRWettstein (Bas63), a myophage in the collection, is a member of the subfamily Ounavirinae and the genus. Using cryo-electron microscopy, we investigated Bas63's structure to explore its evolutionary relationships and functional adaptations. Our structures reveal a series of gene products: (i) a capsid decorated with β-tulip proteins at three-fold symmetry axes and a Hoc-like protein at hexamer centers, (ii) a conserved connector with an additional 12-fold ring of collar proteins that extend unique whisker proteins that are structurally related to podophage GP4 tail fibers, and (iii) a baseplate with long tail fibers resembling a contracted form of T4's long tail fibers. Sequence conservation analysis of Bas63 structural proteins across ICTV-recognized supports its role as a structural model for evolution. This study advances the mechanistic understanding of phage architecture and reinforces the structural mosaicism of bacteriophages.

PubMed: 41223280
DOI: 10.1126/sciadv.adx0790

Experimental method

ELECTRON MICROSCOPY (3.17 Å)