ArticleProceedings of the National Academy of Sciences of the United States of America2017
Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Article
- Proteomic Analysis of Marine Bacteriophages: Structural Conservation, Post-Translational Modifications, and Phage-Host Interactions.Environmental microbiology · 2025Article
- Structure and proposed DNA delivery mechanism of a marine roseophage.Nature communications · 2023Article
- A structural dendrogram of the actinobacteriophage major capsid proteins provides important structural insights into the evolution of capsid stability.Structure (London, England : 1993) · 2023Article
- High-resolution cryo-EM structure of theScience advances · 2022Article
- A Capsid Structure ofViruses · 2022Article
- Polymorphism in peptide self-assembly visualized.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Capsid Structure ofJournal of virology · 2021Article
- High Resolution Structure of the Mature Capsid ofInternational journal of molecular sciences · 2021Article
- High resolution single particle Cryo-EM refinement using JSPR.Progress in biophysics and molecular biology · 2021Review
- CryoEM structure of the tegumented capsid of Epstein-Barr virus.Cell research · 2020Article
- Ecology, Structure, and Evolution ofAnnual review of virology · 2020Review
- Capsid expansion of bacteriophage T5 revealed by high resolution cryoelectron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Principles for enhancing virus capsid capacity and stability from a thermophilic virus capsid structure.Nature communications · 2019Article
- Article
- Conservation and Divergence of the I-Domain Inserted into the Ubiquitous HK97 Coat Protein Fold in P22-Like Bacteriophages.Journal of virology · 2019Article
- Atomic cryo-EM structures of viruses.Current opinion in structural biology · 2017Review
- Flexible Connectors between Capsomer Subunits that Regulate Capsid Assembly.Journal of molecular biology · 2017Article
- Analysis of β-strand Twist from the 3-dimensional Image of a Protein.ACM-BCB ... ... : the ... ACM Conference on Bioinformatics, Computational Biology and Biomedicine. ACM Conference on Bioinformatics, Computational Biology and Biomedicine · 2017Article
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7 authors.
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Abstract
The enormous prevalence of tailed DNA bacteriophages on this planet is enabled by highly efficient self-assembly of hundreds of protein subunits into highly stable capsids. These capsids can stand with an internal pressure as high as ∼50 atmospheres as a result of the phage DNA-packaging process. Here we report the complete atomic model of the headful DNA-packaging bacteriophage Sf6 at 2.9 Å resolution determined by electron cryo-microscopy. The structure reveals the DNA-inflated, tensed state of a robust protein shell assembled via noncovalent interactions. Remarkable global conformational polymorphism of capsid proteins, a network formed by extended N arms, mortise-and-tenon-like intercapsomer joints, and abundant β-sheet-like mainchain:mainchain intermolecular interactions, confers significant strength yet also flexibility required for capsid assembly and DNA packaging. Differential formations of the hexon and penton are mediated by a drastic α-helix-to-β-strand structural transition. The assembly scheme revealed here may be common among tailed DNA phages and herpesviruses.
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