Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus

doi:10.1016/j.bbagen.2018.08.017

CORC > 海洋研究所 > 中国科学院海洋研究所

	Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus
	Liu, Wenxia 1; Liu, Aijun 2,3; Gao, Hailong 2,4; Wang, Quan 2; Wang, Limin 5; Warkentin, Eberhard 1; Rao, Zihe 2,3; Michel, Hartmut 1; Peng, Guohong 1,2,6,7
刊名	BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
	2018-12-01
卷号	1862 期号:12 页码:2797-2805
关键词	Peroxidase AhpC2 1-Cys peroxiredoxins C-terminal region Sulfonic acid form Oligomerization
ISSN号	0304-4165
DOI	10.1016/j.bbagen.2018.08.017
通讯作者	Michel, Hartmut(hartmut.michel@biophys.mpg.de) ; Peng, Guohong(guohong.peng@biophys.mpg.de)
英文摘要	Peroxiredoxins (Prxs) are thiol peroxidases that scavenge various peroxide substrates such as hydrogen peroxide (H2O2), alkyl hydroperoxides and peroxinitrite. They also function as chaperones and are involved in signal transduction by H2O2 in eukaryotic cells. The genome of Aquifex aeolicus, a microaerophilic, hyperthermophilic eubacterium, encodes four Prxs, among them an alkyl hydroperoxide reductase AhpC2 which was found to be closely related to archaeal 1-Cys peroxiredoxins. We determined the crystal structure of AhpC2 at 1.8 angstrom resolution and investigated its oligomeric state in solution by electron microscopy. AhpC2 is arranged as a toroid-shaped dodecamer instead of the typically observed decamer. The basic folding topology and the active site structure are conserved and possess a high structural similarity to other 1-Cys Prxs. However, the C-terminal region adopts an opposite orientation. AhpC2 contains three cysteines, Cys(49), Cys(212), and Cys(218). The peroxidatic cysteine C-p(49) was found to be hyperoxidized to the sulfonic acid (-SO3H) form, while Cys(212) forms an intra-monomer disulfide bond with Cys(218). Mutagenesis experiments indicate that Cys(212) and Cys(218) play important roles in the oligomerization of AhpC2. Based on these structural characteristics, we proposed the catalytic mechanism of AhpC2. This study provides novel insights into the structure and reaction mechanism of 1-Cys peroxiredoxins.
资助项目	Deutsche Forschungsgemeinschaft[SFB 628] ; Deutsche Forschungsgemeinschaft (Cluster of Excellence Macromolecular Complexes Frankfurt) ; Max-Planck-Gesellschaft
WOS研究方向	Biochemistry & Molecular Biology ; Biophysics
语种	英语
出版者	ELSEVIER SCIENCE BV
WOS记录号	WOS:000449240400026
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/156379]
专题	中国科学院海洋研究所
通讯作者	Michel, Hartmut; Peng, Guohong
作者单位	1.Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60438 Frankfurt, Germany 2.Chinese Acad Sci, CAS Ctr Excellence Macromol, Inst Biophys, Natl Lab Biomacromol, Beijing 100101, Peoples R China 3.Tsinghua Univ, Sch Med, Beijing 100084, Peoples R China 4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 5.Chinese Acad Sci, Inst Microbiol, Beijing 100101, Peoples R China 6.Hisun Pharmaceut Hangzhou Co Ltd, Hangzhou 311404, Zhejiang, Peoples R China 7.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China
推荐引用方式 GB/T 7714	Liu, Wenxia,Liu, Aijun,Gao, Hailong,et al. Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus[J]. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS,2018,1862(12):2797-2805.
APA	Liu, Wenxia.,Liu, Aijun.,Gao, Hailong.,Wang, Quan.,Wang, Limin.,...&Peng, Guohong.(2018).Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus.BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS,1862(12),2797-2805.
MLA	Liu, Wenxia,et al."Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus".BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS 1862.12(2018):2797-2805.