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9MT4

Connector structure of phage JohannRWettstein (Bas63)

Summary for 9MT4
Entry DOI10.2210/pdb9mt4/pdb
EMDB information48599
DescriptorPortal protein, Head-closure protein, Tail terminator protein, ... (8 entities in total)
Functional Keywordsconnector, portal, adaptor, head completion, tail terminator, fiber, whisker, collar, tube, sheath, phage, bacteriophage, neck, bas63, johannrwettstein, viral protein
Biological sourceEscherichia phage JohannRWettstein
More
Total number of polymer chains18
Total formula weight419659.00
Authors
Hodgkinson-Bean, J. (deposition date: 2025-01-10, release date: 2025-11-19, Last modification date: 2025-11-26)
Primary citationHodgkinson-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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

245663

數據於2025-12-03公開中

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