Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function

doi:10.1016/j.ecolmodel.2017.04.012

CORC > 植物研究所 > 中国科学院植物研究所 > 中科院光生物学重点实验室

	Structure of the Arabidopsis thaliana NADPH-cytochrome P450 reductase 2 (ATR2) provides insight into its function
	Niu, Guoqi ; Zhao, Shun 2,3; Wang, Lei ; Dong, Wei 2,3; Liu, Lin 2; He, Yikun
刊名	FEBS JOURNAL
	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
电子版国际标准刊号	1742-4658
出版地	HOBOKEN
WOS关键词	ELECTRON-TRANSFER ; STRUCTURE REFINEMENT ; CRYSTAL-STRUCTURE ; ESCHERICHIA-COLI ; OXIDOREDUCTASE ; EXPRESSION ; PLANT ; FMN ; FLAVOPROTEIN ; SUGGESTS
语种	英语
出版者	WILEY
WOS记录号	WOS:000402345800009
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]
内容类型	期刊论文
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.Univ Chinese Acad Sci, Beijing, Peoples R China 2.Capital Normal Univ, Coll Life Sci, 105 Xisanhuan North Rd, Beijing 100048, Peoples R China 3.Chinese Acad Sci, Inst Bot, CAS Ctr Excellence Mol Plant Sci, Key Lab Photobiol, 20 Nanxincun, Beijing 100093, 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.