首页    期刊浏览 2024年11月08日 星期五
登录注册

文章基本信息

  • 标题:The proteasomal subunit Rpn6 is a molecular clamp holding the core and regulatory subcomplexes together
  • 本地全文:下载
  • 作者:Ganesh Ramnath Pathare ; István Nagy ; Stefan Bohn
  • 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:2012
  • 卷号:109
  • 期号:1
  • 页码:149-154
  • DOI:10.1073/pnas.1117648108
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:Proteasomes execute the degradation of most cellular proteins. Although the 20S core particle (CP) has been studied in great detail, the structure of the 19S regulatory particle (RP), which prepares ubiquitylated substrates for degradation, has remained elusive. Here, we report the crystal structure of one of the RP subunits, Rpn6, and we describe its integration into the cryo-EM density map of the 26S holocomplex at 9.1 A resolution. Rpn6 consists of an -solenoid-like fold and a proteasome COP9/signalosome eIF3 (PCI) module in a right-handed suprahelical configuration. Highly conserved surface areas of Rpn6 interact with the conserved surfaces of the Pre8 (alpha2) and Rpt6 subunits from the alpha and ATPase rings, respectively. The structure suggests that Rpn6 has a pivotal role in stabilizing the otherwise weak interaction between the CP and the RP.
  • 关键词:26S proteasome ; cryoelectron microscopy ; PSMD11 ; S9 ; PCI domain
国家哲学社会科学文献中心版权所有