首页    期刊浏览 2024年12月11日 星期三
登录注册

文章基本信息

  • 标题:Structure of a headful DNA-packaging bacterial virus at 2.9 Å resolution by electron cryo-microscopy
  • 本地全文:下载
  • 作者:Haiyan Zhao ; Kunpeng Li ; Anna Y. Lynn
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:2017
  • 卷号:114
  • 期号:14
  • 页码:3601-3606
  • DOI:10.1073/pnas.1615025114
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要: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.
  • 关键词:virus assembly ; bacteriophage ; DNA packaging ; atomic structure ; cryoEM
国家哲学社会科学文献中心版权所有