Crystal Structure of DNA Cytidine Deaminase ABOBEC3G Catalytic Deamination Domain Suggests a Binding Mode of Full-length Enzyme to Single-stranded DNA

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	Crystal Structure of DNA Cytidine Deaminase ABOBEC3G Catalytic Deamination Domain Suggests a Binding Mode of Full-length Enzyme to Single-stranded DNA
	Lu XX(卢秀秀)1; Zhang TL(张天龙)1; Xu Z(徐增)1; Liu SS(刘珊珊)1; Zhao B(赵玢)1; Lan WX(蓝文贤)1; Wang CX(王春喜)1; Ding JP(丁建平)1; Cao CY(曹春阳)1
刊名	J. Biol. Chem.
	2015
卷号	290 期号:7 页码:4010-4021
其他题名	DNA胞嘧啶脱氨基化酶APOBEC3G催化结构域晶体结构揭示全长蛋白结合DNA的模式
通讯作者	曹春阳
英文摘要	APOBEC3G (A3G) is a DNA cytidine deaminase (CD) that demonstrates antiviral activity against human immunodeficiency virus 1 (HIV-1) and other pathogenic virus. It has an inactive N-terminal CD1 virus infectivity factor (Vif) protein binding domain (A3G-CD1) and an actively catalytic C-terminal CD2 deamination domain (A3G-CD2). Although many studies on the structure of A3G-CD2 and enzymatic properties of full-length A3G have been reported, the mechanism of how A3G interacts with HIV-1 single-stranded DNA (ssDNA) is still not well characterized. Here, we reported a crystal structure of a novel A3G-CD2 head-to-tail dimer (in which the N terminus of the monomer H (head) interacts with the C terminus of monomer T (tail)), where a continuous DNA binding groove was observed. By constructing the A3G-CD1 structural model, we found that its overall fold was almost identical to that of A3G-CD2. We mutated the residues located in or along the groove in monomer H and the residues in A3G-CD1 that correspond to those seated in or along the groove in monomer T. Then, by performing enzymatic assays, we confirmed the reported key elements and the residues in A3G necessary to the catalytic deamination. Moreover, we identified more than 10 residues in A3G essential to DNA binding and deamination reaction. Therefore, this dimer structure may represent a structural model of full-length A3G, which indicates a possible binding mode of A3G to HIV-1 ssDNA.
学科主题	生命有机化学
收录类别	SCI
原文出处	http://dx.doi.org/10.1074/jbc.M114.624262
语种	英语
WOS记录号	WOS:000349458400014
内容类型	期刊论文
源URL	[http://ir.sioc.ac.cn/handle/331003/39489]
专题	上海有机化学研究所_生命有机化学国家重点实验室
作者单位	1.中科院上海有机化学研究所, 生命有机化学国家重点实验室 2.中科院上海生命科学研究院
推荐引用方式 GB/T 7714	Lu XX,Zhang TL,Xu Z,et al. Crystal Structure of DNA Cytidine Deaminase ABOBEC3G Catalytic Deamination Domain Suggests a Binding Mode of Full-length Enzyme to Single-stranded DNA[J]. J. Biol. Chem.,2015,290(7):4010-4021.
APA	卢秀秀.,张天龙.,徐增.,刘珊珊.,赵玢.,...&曹春阳.(2015).Crystal Structure of DNA Cytidine Deaminase ABOBEC3G Catalytic Deamination Domain Suggests a Binding Mode of Full-length Enzyme to Single-stranded DNA.J. Biol. Chem.,290(7),4010-4021.
MLA	卢秀秀,et al."Crystal Structure of DNA Cytidine Deaminase ABOBEC3G Catalytic Deamination Domain Suggests a Binding Mode of Full-length Enzyme to Single-stranded DNA".J. Biol. Chem. 290.7(2015):4010-4021.