Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
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DOI：
10.1038/385176a0
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发表时间：
1997-01-09
期刊：
影响因子：
64.8
通讯作者：
Frappier, L
中科院分区：
文献类型：
--
作者：
Bochkarev, A;Pfuetzner, RA;Frappier, L
单链 DNA 结合蛋白 (SSB) 是原核和真核细胞、线粒体、噬菌体和病毒中必不可少的 DNA 功能 (1,2)。四种 SSB 的结构已被解析(3-7)，但 SSB 与 DNA 相互作用的分子细节仍然是推测性的。我们在此报告了与 DNA 结合的人类复制蛋白 A (RPA) 的单链 DNA 结合结构域的晶体结构，分辨率为 2.4 埃。复制蛋白a是一种异三聚体SSB，在真核生物中高度保守。最大的亚基 RPA70 与单链 (ss)DNA (8,9) 结合，并介导与许多细胞和病毒蛋白的相互作用 (10)。 DNA 结合结构域连接在 RPA70 的中间，包含两个串联的结构同源子结构域。单链 DNA 位于从一个子域延伸到另一个子域的通道中。每个 RPA70 子结构域的结构与噬菌体 SSB 的结构相似，表明 ssDNA 结合机制是保守的。
THE single-stranded-DNA-binding proteins (SSBs) are essential fur DNA function in prokaryotic and eukaryotic cells, mitochondria, phages and viruses(1,2). The structures of four SSBs have been solved(3-7), but the molecular details of the interaction of SSBs with DNA remain speculative. We report here the crystal structure at 2.4 Angstrom resolution of the single-stranded-DNA-binding domain of human replication protein A (RPA) bound to DNA. Replication protein a is a heterotrimeric SSB that is highly conserved in eukaryotes. The largest subunit, RPA70, binds to single-stranded (ss)DNA(8,9) and mediates interactions with many cellular and viral proteins(10). The DNA-binding domain, which ties in the middle of RPA70, comprises two structurally homologous subdomains oriented in tandem. The ssDNA lies in a channel that extends from one subdomain lo the other. The structure of each RPA70 subdomain is similar to those of the bacteriophage SSBs, indicating that the mechanism of ssDNA-binding is conserved.