Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA

被引：488

作者：

Bochkarev, A ^{[1
]}

Pfuetzner, RA ^{[1
]}

Edwards, AM ^{[1
]}

Frappier, L ^{[1
]}

机构：

[1] MCMASTER UNIV,INST MOL BIOL & BIOTECHNOL,CANC RES GRP,HAMILTON,ON L8N 3Z5,CANADA

来源：

NATURE | 1997年 / 385卷 / 6612期

关键词：

D O I：

10.1038/385176a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：176 / 181

页数：6

共 24 条

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