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-Structure paper
タイトル | Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 114, Issue 14, Page 3601-3606, Year 2017 |
掲載日 | 2017年4月4日 |
著者 | Haiyan Zhao / Kunpeng Li / Anna Y Lynn / Keith E Aron / Guimei Yu / Wen Jiang / Liang Tang / |
PubMed 要旨 | 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. |
リンク | Proc Natl Acad Sci U S A / PubMed:28320961 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.89 Å |
構造データ | |
化合物 | ChemComp-CL: |
由来 |
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キーワード | VIRUS / phage / Sf6 |