Crystal structure of the TLDc domain of oxidation resistance protein 2 from zebrafish

被引:37
作者
Blaise, Mickael [1 ]
Alsarraf, Husam M. A. B. [1 ]
Wong, Jaslyn E. M. M. [1 ]
Midtgaard, Soren Roi [2 ]
Laroche, Fabrice [1 ,3 ]
Schack, Lotte [1 ]
Spaink, Herman [1 ,3 ]
Stougaard, Jens [1 ]
Thirup, Soren [1 ]
机构
[1] Aarhus Univ, Ctr Carbohydrate Recognit & Signalling, Dept Mol Biol & Genet, Aarhus, Denmark
[2] Univ Copenhagen, Fac Life Sci, Nanobiosci Grp, Copenhagen, Denmark
[3] Leiden Univ, Inst Biol, Leiden, Netherlands
基金
新加坡国家研究基金会;
关键词
oxidation resistance; Ncoa7; ERAP140; TBC1D24; TLDc; reactive oxygen species; FAMILY; PHENIX;
D O I
10.1002/prot.24050
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
The oxidation resistance proteins (OXR) help to protect eukaryotes from reactive oxygen species. The sole C-terminal domain of the OXR, named TLDc is sufficient to perform this function. However, the mechanism by which oxidation resistance occurs is poorly understood. We present here the crystal structure of the TLDc domain of the oxidation resistance protein 2 from zebrafish. The structure was determined by X-ray crystallography to atomic resolution (0.97 angstrom) and adopts an overall globular shape. Two antiparallel beta-sheets form a central beta-sandwich, surrounded by two helices and two one-turn helices. The fold shares low structural similarity to known structures. Proteins 2012. (c) 2012 Wiley Periodicals, Inc.
引用
收藏
页码:1694 / 1698
页数:5
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