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
Rok vydání: 2017
Předmět:
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