The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding
The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding
复制标题
DOI：
10.1074/jbc.m406780200
复制
发表时间：
2005-01-28
影响因子：
4.8
通讯作者：
Tucker, PA
中科院分区：
文献类型：
--
作者：
Mapelli, M;Panjikar, S;Tucker, PA
包括动物病毒在内的所有生物在DNA复制过程中都使用特定的蛋白质以非序列特异性的、灵活的和合作的方式快速结合单链DNA。在3.0埃分辨率下测定了单纯疱疹病毒1型主要单链DNA结合蛋白ICP8的60个残基的C末端缺失结构。该结构揭示了一个新的折叠，由一个大的N-末端结构域(残基9-1038)和一个小的C-末端结构域(残基1049-1129)组成。根据晶体的结构和最近邻相互作用，我们提出了一个描述单链DNA结合位置的模型，并解释了协同结合的基础。该模型与电子显微镜下观察到的珠状形貌相吻合。
All organisms including animal viruses use specific proteins to bind single-stranded DNA rapidly in a non-sequence-specific, flexible, and cooperative manner during the DNA replication process. The crystal structure of a 60-residue C-terminal deletion construct of ICP8, the major single-stranded DNA-binding protein from herpes simplex virus-1, was determined at 3.0 Angstrom resolution. The structure reveals a novel fold, consisting of a large N-terminal domain (residues 9-1038) and a small C-terminal domain (residues 1049-1129). On the basis of the structure and the nearest neighbor interactions in the crystal, we have presented a model describing the site of single-stranded DNA binding and explaining the basis for cooperative binding. This model agrees with the beaded morphology observed in electron micrographs.