SSB | |||||||||
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Crystal structure of PriB- a primosomal DNA replication protein of Escherichia coli
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Identifiers | |||||||||
Symbol | SSB | ||||||||
Pfam | PF00436 | ||||||||
Pfam clan | CL0021 | ||||||||
InterPro | IPR000424 | ||||||||
PROSITE | PDOC00602 | ||||||||
SCOP | 1kaw | ||||||||
SUPERFAMILY | 1kaw | ||||||||
TCDB | 3.A.7 | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Viral_DNA_bp | |||||||||
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Single stranded DNA-binding protein(icp8) from herpes simplex virus-1
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Identifiers | |||||||||
Symbol | Viral_DNA_bp | ||||||||
Pfam | PF00747 | ||||||||
InterPro | IPR000635 | ||||||||
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Available protein structures: | |
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Pfam | structures |
PDB | RCSB PDB; PDBe; PDBj |
PDBsum | structure summary |
Replication protein A
(heterotrimer) |
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This is an image of human Replication protein A. From PDB: 1L1O Proteopedia 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.