Solution structure of Escherichia coli HypC
- 影响因子：
0.0
- 发表刊物：
Biochem. Biophys. Res. Commun.
- 摘要：
Escherichia coli HypC plays an important role in the maturation process of the pre-maturated HycE, the large subunit of hydrogenase 3. It serves as an iron transfer as well as a chaperone protein during the maturation process of pre-HycE, and interacts with both HypD and HycE. The N-terminal cysteine residue of HypC plays a key role in the protein-protein interactions. Here, we present the three-dimensional structure of E. coli HypC, the first solution structure of HupF/HypC family. Our result demonstrates that E. coli HypC consists of a typical OB-fold beta-barrel with two C-terminal helixes. Sequence alignment and structural comparison reveal that the hydrophobic region on the surface of E. coli HypC, as well as the highly flexible C-terminal helixes, may involve in the interactions of E. coli HypC with other proteins.
- 论文类型：
期刊论文
- 论文编号：
16
- 卷号：
361
- 期号：
3
- 页面范围：
665-669
- 是否译文：
否
- 发表时间：
2007-09-28
- 发布期刊链接：
- 第一作者：
Wang Lei
- 通讯作者：
Jin Changwen
- 全部作者：
Xia Bin
