Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form
Crystal structure of the homologous-pairing domain from the human Rad52 recombinase in the undecameric form
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DOI：
10.1016/s1097-2765(02)00587-7
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发表时间：
2002-08-01
期刊：
影响因子：
16
通讯作者：
Yokoyama, S
中科院分区：
文献类型：
--
作者：
Kagawa, W;Kurumizaka, H;Yokoyama, S
人Rad 52蛋白形成催化同源配对的七聚体环。Rad 52的N-末端一半是用于同源配对的催化结构域，并且据报道由结构域片段形成的环大约是十聚体的。Rad 52的剪接变体和酵母同源物（Rad 59）主要由该结构域组成。在这项研究中，我们确定了人Rad 52同源配对结构域的晶体结构，并揭示了该结构域形成十一聚体环。每个单体具有β-α折叠，其由Rad 52同源物中高度保守的氨基酸残基组成。突变分析显示，位于β-β-β-α折叠和特征发夹环之间的氨基酸残基对于ssDNA和dsDNA结合是必需的。
The human Rad52 protein forms a heptameric ring that catalyzes homologous pairing. The N-terminal half of Rad52 is the catalytic domain for homologous pairing and the ring formed by the domain fragment was reported to be approximately decameric. Splicing variants of Rad52 and a yeast homolog (Rad59) are composed mostly of this domain. In this study, we determined the crystal structure of the homologous-pairing domain of human Rad52 and revealed that the domain forms an undecameric ring. Each monomer has a beta-beta-beta-alpha fold, which consists of highly conserved amino acid residues among Rad52 homologs. A mutational analysis revealed that the amino acid residues located between the beta-beta-beta-alpha fold and the characteristic hairpin loop are essential for ssDNA and dsDNA binding.