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Single-stranded binding protein

SSB
PDB 1v1q EBI.jpg
Crystal structure of PriB- a primosomal DNA replication protein of Escherichia coli
Identifiers
Symbol SSB
Pfam PF00436
Pfam clan CL0021
InterPro IPR000424
PROSITE PDOC00602
SCOP 1kaw
SUPERFAMILY 1kaw
TCDB 3.A.7
Viral_DNA_bp
PDB 1urj EBI.jpg
Single stranded DNA-binding protein(icp8) from herpes simplex virus-1
Identifiers
Symbol Viral_DNA_bp
Pfam PF00747
InterPro IPR000635
Replication protein A
(heterotrimer)
1L1O Replication protein A.png
This is an image of human Replication protein A. From PDB: 1L1OProteopedia protein A Replication protein A
Subunit
name
Gene Chromosomal
locus
Replication protein A1 RPA1 Chr. 17 p13.3
Replication protein A2 RPA2 Chr. 1 p35.3
Replication protein A3 RPA3 Chr. 7 p21.3

Single-stranded binding proteins (SSBPs) are a class of proteins that have been identified in both viruses and organisms from bacteria to humans.

Binds to single stranded DNA and prevent it from re-forming a double stranded structure

Although the overall picture of human cytomegalovirus (HHV-5) DNA synthesis appears typical of the herpesviruses, some novel features are emerging.

In ICP8, the herpes simplex virus (HSV-1) single-strand DNA-binding protein (ssDNA-binding protein (SSB)), the head consists of the eight alpha helices. The front side of the neck region consists of a five-stranded beta-sheet and two alpha helices, whereas the back side is a three-stranded beta-sheet The shoulder part of the N-terminal domain contains an alpha-helical and beta-sheet region. The herpes simplex virus (HSV-1) SSB, ICP8, is a nuclear protein that, along other replication proteins is required for viral DNA replication during lytic infection.

Six herpes virus-group-common genes encode proteins that likely constitute the replication fork machinery, including a two-subunit DNA polymerase, a Helicase-primase complex and a single-stranded DNA-binding protein. The human herpesvirus 1 (HHV-1) single-strand DNA-binding protein ICP8 is a 128kDa zinc metalloprotein. Photoaffinity labeling has shown that the region encompassing amino acid residues 368-902 contains the single-strand DNA-binding site of ICP8. The HHHV-1 UL5, UL8, and UL52 genes encode an essential heterotrimeric DNA helicase-primase that is responsible for concomitant DNA unwinding and primer synthesis at the viral DNA replication fork. ICP8 may stimulate DNA unwinding and enable bypass of cisplatin damaged DNA by recruiting the helicase-primase to the DNA.


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