Summary information and primary citation
- PDB-id
-
1jmc;
DSSR-derived features in text and
JSON formats
- Class
- replication-DNA
- Method
- X-ray (2.4 Å)
- Summary
- Single stranded DNA-binding domain of human replication
protein a bound to single stranded DNA, rpa70 subunit,
residues 183-420
- Reference
-
Bochkarev A, Pfuetzner RA, Edwards AM, Frappier L (1997):
"Structure
of the single-stranded-DNA-binding domain of replication
protein A bound to DNA." Nature,
385, 176-181. doi: 10.1038/385176a0.
- Abstract
- The single-stranded-DNA-binding proteins (SSBs) are
essential for DNA function in prokaryotic and eukaryotic
cells, mitochondria, phages and viruses. The structures of
four SSBs have been solved, but the molecular details of
the interaction of SSBs with DNA remain speculative. We
report here the crystal structure at 2.4 A 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 and mediates interactions with many cellular and
viral proteins. The DNA-binding domain, which lies in the
middle of RPA70, comprises two structurally homologous
subdomains oriented in tandem. The ssDNA lies in a channel
that extends from one subdomain to 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.
