期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 107, 期 24, 页码 10884-10889出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1003015107
关键词
protein biosynthesis; virus
资金
- Danish Science Research Council, Danscatt
- Vilhelm Petersen foundation
- Danish National Research Foundation
- Novo-Nordisk foundation
- Russian Foundation for Basic Research
- Russian Academy of Sciences
The RNA-dependent RNA polymerase core complex formed upon infection of Escherichia coli by the bacteriophage Q beta is composed of the viral catalytic beta-subunit as well as the host translation elongation factors EF-Tu and EF-Ts, which are required for initiation of RNA replication. We have determined the crystal structure of the complex between the beta-subunit and the two host proteins to 2.5-angstrom resolution. Whereas the basic catalytic machinery in the viral subunit appears similar to other RNA-dependent RNA polymerases, a unique C-terminal region of the beta-subunit engages in extensive interactions with EF-Tu and may contribute to the separation of the transient duplex formed between the template and the nascent product to allow exponential amplification of the phage genome. The evolution of resistance by the host appears to be impaired because of the interactions of the beta-subunit with parts of EF-Tu essential in recognition of aminoacyl-tRNA.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据