Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function
文献类型：期刊论文
| 作者 | Niu, Guoqi; Zhao, Shun1,2; Wang, Lei ; Dong, Wei1,2; Liu, Lin1; He, Yikun
|
| 刊名 | FEBS JOURNAL
 |
| 出版日期 | 2017 |
| 卷号 | 284期号:5页码:754-765 |
| 关键词 | conformational change crystallography electron transfer flavoprotein reduction/oxidation |
| ISSN号 | 1742-464X |
| DOI | 10.1016/j.ecolmodel.2017.04.012 |
| 文献子类 | Article |
| 英文摘要 | Members of the cytochrome P450 family catalyze a variety of mono-oxygenase reactions, and for the eukaryotic membrane-bound members, NADPH is typically used as the reducing agent. The flavoprotein NADPH-cytochrome P450 reductase (CPR) enables electron transfer from NADPH to cytochrome P450 via its flavin cofactors. ATR2 is one of the two authentic CPR genes in the genome of the model plant Arabidopsis thaliana, and its product has been physiologically and kinetically characterized. Here, we report the 2.3 angstrom structure of Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) and find that the position of the two flavin cofactors differs from that of other known CPR structures. Mutation of residues related to possible interflavin electron transfer retains the reductase activity of ATR2, which suggests a direct electron transfer pathway between the flavins. In contrast, mutation of a single residue (R708) mediating interdomain interaction abolishes this activity. Because this residue is only conserved in plant CPRs, we speculate a plant-specific working mechanism as observed in ATR2. |
| 学科主题 | Environmental Sciences & Ecology |
| 出版地 | HOBOKEN |
| 电子版国际标准刊号 | 1742-4658 |
| WOS关键词 | ELECTRON-TRANSFER ; STRUCTURE REFINEMENT ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; OXIDOREDUCTASE ; EXPRESSION ; PLANT ; FMN ; FLAVOPROTEIN ; SUGGESTS |
| 语种 | 英语 |
| WOS记录号 | WOS:000402345800009 |
| 出版者 | WILEY |
| 资助机构 | National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [31670794, 31530006] ; Strategic Priority Research Program of Chinese Academy of SciencesChinese Academy of Sciences [XDB17030300] |
| 源URL | [http://ir.ibcas.ac.cn/handle/2S10CLM1/22230]  |
| 专题 | 中科院光生物学重点实验室 |
| 作者单位 | 1.Capital Normal Univ, Coll Life Sci, 105 Xisanhuan North Rd, Beijing 100048, Peoples R China 2.Chinese Acad Sci, Inst Bot, CAS Ctr Excellence Mol Plant Sci, Key Lab Photobiol, 20 Nanxincun, Beijing 100093, Peoples R China 3.Univ Chinese Acad Sci, Beijing, Peoples R China |
| 推荐引用方式 GB/T 7714 | Niu, Guoqi,Zhao, Shun,Wang, Lei,et al. Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function[J]. FEBS JOURNAL,2017,284(5):754-765. |
| APA | Niu, Guoqi,Zhao, Shun,Wang, Lei,Dong, Wei,Liu, Lin,&He, Yikun.(2017).Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function.FEBS JOURNAL,284(5),754-765. |
| MLA | Niu, Guoqi,et al."Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function".FEBS JOURNAL 284.5(2017):754-765. |
入库方式： OAI收割
来源：植物研究所
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