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

doi:10.1016/j.bbagen.2018.08.017

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	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
	2018-12-01
发表期刊	BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
ISSN	0304-4165
卷号	1862 期号:12 页码:2797-2805
通讯作者	Michel, Hartmut([email protected]) ; Peng, Guohong([email protected])
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.
关键词	Peroxidase AhpC2 1-Cys peroxiredoxins C-terminal region Sulfonic acid form Oligomerization
DOI	10.1016/j.bbagen.2018.08.017
收录类别	SCI
语种	英语
资助项目	Deutsche Forschungsgemeinschaft[SFB 628]###834; Deutsche Forschungsgemeinschaft (Cluster of Excellence Macromolecular Complexes Frankfurt)###835; Max-Planck-Gesellschaft###836; Deutsche Forschungsgemeinschaft[SFB 628]; Deutsche Forschungsgemeinschaft (Cluster of Excellence Macromolecular Complexes Frankfurt); Max-Planck-Gesellschaft
WOS研究方向	Biochemistry & Molecular Biology ; Biophysics
WOS类目	Biochemistry & Molecular Biology ; Biophysics
WOS记录号	WOS:000449240400026
出版者	ELSEVIER SCIENCE BV
引用统计	被引频次：4[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	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
通讯作者单位	中国科学院海洋研究所
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.

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