Conformational Dynamics of the Periplasmic Chaperone SurA.
- 影响因子：
0.0
- DOI码：
10.1021/acs.biochem.0c00507
- 发表刊物：
Biochemistry
- 摘要：
The periplasmic protein SurA is the primary chaperone involved in the biogenesis of bacterial outer membrane proteins and is a potential antibacterial drug target. The three-dimensional structure of SurA can be divided into three parts, a core module formed by the N- and C-terminal regions and two peptidyl-prolyl isomerase (PPIase) domains, P1 and P2. Despite the determination of the structures of several SurA-peptide complexes, the functional mechanism of this chaperone remains elusive and the roles of the two PPIase domains are yet unclear. Herein, we characterize the conformational dynamics of SurA by using solution nuclear magnetic resonance and single-molecule fluorescence resonance energy transfer methods. We demonstrate a "closed-to-open" structural transition of the P1 domain that is correlated with both chaperone activity and peptide binding and show that the flexible P2 domain can also occupy conformations that closely contact the NC core module. Our results offer a structural basis for the counteracting roles of the two PPIase domains in regulating the SurA chaperone activity.
- 论文类型：
期刊论文
- 论文编号：
65
- 文献类型：
J
- 卷号：
59
- 期号：
35
- 页面范围：
3235-3246
- 是否译文：
否
- 发表时间：
2020-09-08
- 收录刊物：
SCI
- 第一作者：
Moye Jia
- 通讯作者：
Changwen Jin,Yunfei Hu
- 全部作者：
Bo Wu,Chunlai Chen,Meiping Zhao,Xianhui Hou,Xiaogang Niu
