IOCAS-IR
Structural properties of the peroxiredoxin AhpC2 from the hyperthermophilic eubacterium Aquifex aeolicus
Liu, Wenxia1; Liu, Aijun2,3; Gao, Hailong2,4; Wang, Quan2; Wang, Limin5; Warkentin, Eberhard1; Rao, Zihe2,3; Michel, Hartmut1; Peng, Guohong1,2,6,7
2018-12-01
Source PublicationBIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
ISSN0304-4165
Volume1862Issue:12Pages:2797-2805
Corresponding AuthorMichel, Hartmut(hartmut.michel@biophys.mpg.de) ; Peng, Guohong(guohong.peng@biophys.mpg.de)
AbstractPeroxiredoxins (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.
KeywordPeroxidase AhpC2 1-Cys peroxiredoxins C-terminal region Sulfonic acid form Oligomerization
DOI10.1016/j.bbagen.2018.08.017
Indexed BySCI
Language英语
Funding ProjectDeutsche Forschungsgemeinschaft[SFB 628] ; Deutsche Forschungsgemeinschaft (Cluster of Excellence Macromolecular Complexes Frankfurt) ; Max-Planck-Gesellschaft
WOS Research AreaBiochemistry & Molecular Biology ; Biophysics
WOS SubjectBiochemistry & Molecular Biology ; Biophysics
WOS IDWOS:000449240400026
PublisherELSEVIER SCIENCE BV
Citation statistics
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/156380
Collection中国科学院海洋研究所
Corresponding AuthorMichel, Hartmut; Peng, Guohong
Affiliation1.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
Corresponding Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Recommended Citation
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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