Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy
Autor: | Anna Y. Lynn, Keith E. Aron, Guimei Yu, Haiyan Zhao, Kunpeng Li, Liang Tang, Wen Jiang |
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Rok vydání: | 2017 |
Předmět: |
Models
Molecular 0301 basic medicine viruses Protein subunit Crystallography X-Ray Protein Structure Secondary Bacteriophage 03 medical and health sciences chemistry.chemical_compound Capsid DNA Packaging Atomic model Non-covalent interactions Bacteriophages chemistry.chemical_classification Multidisciplinary 030102 biochemistry & molecular biology biology Virus Assembly Cryoelectron Microscopy Resolution (electron density) Biological Sciences biology.organism_classification Crystallography 030104 developmental biology chemistry Biophysics Capsid Proteins Bacterial virus DNA |
Zdroj: | Proceedings of the National Academy of Sciences. 114:3601-3606 |
ISSN: | 1091-6490 0027-8424 |
DOI: | 10.1073/pnas.1615025114 |
Popis: | 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. |
Databáze: | OpenAIRE |
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