Crystal structure of the DNA-Binding domain of the Epstein-Barr virus origin-binding protein, EBNA1, bound to DNA
Crystal structure of the DNA-Binding domain of the Epstein-Barr virus origin-binding protein, EBNA1, bound to DNA
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DOI：
10.1016/s0092-8674(00)81056-9
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发表时间：
1996-03-08
期刊：
影响因子：
64.5
通讯作者：
Edwards, AM
中科院分区：
文献类型：
--
作者：
Bochkarev, A;Barwell, JA;Edwards, AM
Epstein-Barr 病毒核抗原 1 (EBNA1) 蛋白结合并激活 oriP 的 DNA 复制，oriP 是 Epstein-Barr 病毒 DNA 复制的潜在起点。以 2.4 埃分辨率解析了与 18 bp 结合位点结合的 EBNA1 DNA 结合域的晶体结构。 EBNA1 包含两个结构域：侧翼结构域和核心结构域。侧翼结构域包括伸入大沟的螺旋和沿着小沟行进的延伸链，它与 DNA 进行所有决定序列的接触。核心结构域在结构上与牛乳头状瘤病毒E2蛋白的完整DNA结合结构域同源，不与DNA碱基直接接触。提出了一种起源解旋模型，该模型结合了 EBNA1-起源相互作用的已知生化和结构特征。
The Epstein-Barr virus nuclear antigen 1 (EBNA1) protein binds to and activates DNA replication from oriP, the latent origin of DNA replication in Epstein-Barr virus. The crystal structure of the DNA-binding domain of EBNA1 bound to an 18 bp binding site was solved at 2.4 Angstrom resolution. EBNA1 comprises two domains, a flanking and a core domain. The flanking domain, which includes a helix that projects into the major groove and an extended chain that travels along the minor groove, makes all of the sequence-determining contacts with the DNA. The core domain, which is structurally homologous to the complete DNA-binding domain of the bovine papilloma virus E2 protein, makes no direct contacts with the DNA bases. A model for origin unwinding is proposed that incorporates the known biochemical and structural features of the EBNA1-origin interaction.