与DNA结合的爱泼斯坦-巴尔病毒起始结合蛋白EBNA1的DNA结合结构域的晶体结构。

Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein, EBNA1, bound to DNA.

作者信息

Bochkarev A, Barwell J A, Pfuetzner R A, Bochkareva E, Frappier L, Edwards A M

机构信息

Institute for Molecular Biology and Biotechnology, Cancer Research Group, Department of Pathology, McMaster University, Hamilton, Ontario Canada.

出版信息

Cell. 1996 Mar 8;84(5):791-800. doi: 10.1016/s0092-8674(00)81056-9.

DOI:10.1016/s0092-8674(00)81056-9

PMID:8625416

Abstract

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 A 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.

摘要

爱泼斯坦-巴尔病毒核抗原1（EBNA1）蛋白与爱泼斯坦-巴尔病毒DNA复制的潜伏起始位点oriP结合并激活DNA复制。以2.4埃的分辨率解析了EBNA1的DNA结合结构域与一个18碱基对结合位点结合的晶体结构。EBNA1由两个结构域组成，一个侧翼结构域和一个核心结构域。侧翼结构域包括一个伸入大沟的螺旋和一个沿小沟延伸的链，它与DNA进行所有序列决定接触。核心结构域在结构上与牛乳头瘤病毒E2蛋白的完整DNA结合结构域同源，不与DNA碱基直接接触。提出了一个起始位点解旋模型，该模型整合了EBNA1与起始位点相互作用的已知生化和结构特征。