ArticleScience advances2023
A symmetry mismatch unraveled: How phage HK97 scaffold flexibly accommodates a 12-fold pore at a 5-fold viral capsid vertex.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
- Something old, something new? Herpesvirus genome packaging examined in light of lessons from the tailed bacteriophages.Journal of virology · 2026Review
- Article
- A highly conserved basic motif in the wing domain of portal protein is necessary for oligomerization and incorporation in phage P22.Journal of virology · 2026Article
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Structural insights into scaffold-guided assembly of the Pseudomonas phage D3 capsid.Nature communications · 2025Article
- Elucidating double stranded DNA viral scaffolding protein structures through advances in cryogenic electron microscopy data processing.Current opinion in structural biology · 2025Review
- Cryo-EM and cryo-ET reveal the molecular architecture and host interactions of mycobacteriophage Douge.Cell reports · 2025Article
- Review
- A Two-Component Pseudo-Icosahedral Protein Nanocompartment with Variable Shell Composition and Irregular Tiling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Structure of the Staphylococcus aureus bacteriophage 80α neck shows details of the DNA, tail completion protein, and tape measure protein.Structure (London, England : 1993) · 2025Article
- Article
- Structure of the scaffolding protein and portal within the bacteriophage P22 procapsid provides insights into the self-assembly process.PLoS biology · 2025Article
- Structure of the Portal Complex from Staphylococcus aureus Pathogenicity Island 1 Transducing Particles In Situ and In Isolation.Journal of molecular biology · 2024Article
- Architecture and Assembly of Structurally Complex Viruses.Sub-cellular biochemistry · 2024Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Tailed bacteriophages and herpesviruses use a transient scaffold to assemble icosahedral capsids with hexameric capsomers on the faces and pentameric capsomers at all but one vertex where a 12-fold portal is thought to nucleate the assembly. How does the scaffold orchestrate this step? We have determined the portal vertex structure of the bacteriophage HK97 procapsid, where the scaffold is a domain of the major capsid protein. The scaffold forms rigid helix-turn-strand structures on the interior surfaces of all capsomers and is further stabilized around the portal, forming trimeric coiled-coil towers, two per surrounding capsomer. These 10 towers bind identically to 10 of 12 portal subunits, adopting a pseudo-12-fold organization that explains how the symmetry mismatch is managed at this early step.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.