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-Structure paper
Title | Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy. |
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Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 114, Issue 14, Page 3601-3606, Year 2017 |
Publish date | Apr 4, 2017 |
Authors | Haiyan Zhao / Kunpeng Li / Anna Y Lynn / Keith E Aron / Guimei Yu / Wen Jiang / Liang Tang / |
PubMed 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 ...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. |
External links | Proc Natl Acad Sci U S A / PubMed:28320961 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.89 Å |
Structure data | |
Chemicals | ChemComp-CL: |
Source |
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Keywords | VIRUS / phage / Sf6 |