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9HU6

Asymmetric unit from transcribing single-layered particle of bacteriophage phi6 in an over-expanded state

Summary for 9HU6
Entry DOI10.2210/pdb9hu6/pdb
EMDB information52401
DescriptorMajor inner protein P1, NTPase (2 entities in total)
Functional Keywordscystovirus, phi6, semi-conservative transcription, cryo-em, cryogenic electron microscopy, localized reconstruction, symmetry relaxation, virus, dsrna virus, bacteriophage
Biological sourceCystovirus phi6
More
Total number of polymer chains3
Total formula weight173701.23
Authors
Ilca, S.L.,Kumpula, E.-P.,Huiskonen, J.T. (deposition date: 2024-12-20, release date: 2026-01-14, Last modification date: 2026-02-04)
Primary citationIlca, S.L.,Sun, X.,Kumpula, E.P.,Eskelin, K.,Stuart, D.I.,Poranen, M.M.,Huiskonen, J.T.
Capsid restructuring activates semi-conservative dsRNA transcription in cystovirus ɸ6.
Mol.Cell, 86:289-, 2026
Cited by
PubMed Abstract: Double-stranded (ds)RNA viruses replicate and transcribe their genome within a proteinaceous viral capsid to evade host cell defenses. While Reovirales members use conservative transcription, most dsRNA viruses, including cystoviruses, utilize semi-conservative transcription, in which a newly synthesized positive strand replaces the parental positive strand, which is released as mRNA. Here, we visualize semi-conservative transcription activation in cystovirus ɸ6 double-layered particles using cryogenic electron microscopy. We observe nucleotide-triggered disassembly of the domain-swapped outer capsid layer, subsequent expansion of the inner capsid layer, and stepwise assembly of transcription complexes at the opposing poles of the spooled dsRNA genome. These complexes consist of the viral polymerases embedded into a triskelion formed by the minor protein P7, which we show as essential for continuous transcription. The packaging hexamers proximal to the transcription sites channel the viral mRNA exit. Our results define the complex molecular pathway from the quiescent state to activated semi-conservative transcription.
PubMed: 41512857
DOI: 10.1016/j.molcel.2025.12.025
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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PDB entries from 2026-03-04

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