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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
Alternative TitleDNA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
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
2015
Source PublicationJ. Biol. Chem.
Volume290Issue:7Pages:4010-4021
AbstractAPOBEC3G (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.
Subtype论文
Subject Area生命有机化学
DOI10.1074/jbc.M114.624262
URL查看原文
Indexed BySCI
Language英语
WOS IDWOS:000349458400014
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Document Type期刊论文
Identifierhttp://ir.sioc.ac.cn/handle/331003/39489
Collection生命有机化学国家重点实验室
Corresponding AuthorCao CY(曹春阳)
Affiliation1.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
Recommended Citation
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.
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