1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli
- 影响因子：
0.0
- 发表刊物：
Biomol. NMR Assign.
- 关键字：
Chaperone; PPIase domain; SurA
- 摘要：
The periplasmic chaperone SurA in Gram-negative bacteria plays a central role in the biogenesis of integral outer membrane proteins and is critical to the maintenance of bacterial membrane integrity. SurA contains a core chaperone module comprising the N- and C-terminal domains, along with two peptidyl-prolyl isomerase (PPIase) domains. The chaperone activity of SurA has been demonstrated to rely on the core module, whereas recent works suggested that the PPIase domains may regulate the chaperone activity through large conformational rearrangements. Herein, we report the resonance assignments of 1H, 13C and 15N atoms of the second PPIase domain of Escherichia coli SurA, which provide valuable information for further studies of the structure, dynamics and interactions of this chaperone using NMR techniques.
- 论文类型：
期刊论文
- 论文编号：
60
- 学科门类：
理学
- 卷号：
13
- 期号：
1
- 页面范围：
183-186
- 是否译文：
否
- 发表时间：
2019-04-01
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Jia Moye
- 通讯作者：
Hu Yunfei,Jin Changwen
