1H, 13C and 15N resonance assignments of the rhodanese domain of YgaP from Escherichia coli
- 影响因子：
0.0
- 发表刊物：
Biomol. NMR Assign.
- 摘要：
Rhodanese domain is a ubiquitous structural module commonly found in bacterial, archaeal and eukaryotic cells. Growing evidence indicates that rhodanese domains act as the carrier of reactive sulfur atoms by forming persulfide intermediates in distinct metabolic pathways. YgaP, a membrane protein consisting of a rhodanese domain and a C-terminal transmembrane segment, is the only membrane-associated rhodanese in Escherichia coli. Herein, we report the resonance assignments of (1)H, (13)C and (15)N atoms of rhodanese domain of YgaP. Totally, chemical shifts of more than 95% of the atoms were assigned.
- 论文类型：
期刊论文
- 论文编号：
35
- 卷号：
5
- 期号：
1
- 页面范围：
101-103
- 是否译文：
否
- 发表时间：
2011-04-04
- 收录刊物：
SCI
- 发布期刊链接：
- 第一作者：
Li Hongwei
- 通讯作者：
Jin Changwen
- 全部作者：
Bi Yunchen,Xia Bin
