Abstract
All organisms including animal viruses use specific proteins to bind single-stranded DNA rapidly in a non-sequence-specific, flexible, and cooperative manner during the DNA replication process. The crystal structure of a 60-residue C-terminal deletion construct of ICP8, the major single-stranded DNA-binding protein from herpes simplex virus-1, was determined at 3.0 A resolution. The structure reveals a novel fold, consisting of a large N-terminal domain (residues 9-1038) and a small C-terminal domain (residues 1049-1129). On the basis of the structure and the nearest neighbor interactions in the crystal, we have presented a model describing the site of single-stranded DNA binding and explaining the basis for cooperative binding. This model agrees with the beaded morphology observed in electron micrographs.
Highlights
Viruses of the Herpesviridae family infect almost all vertebrates, including man, causing a variety of diseases
Of the seven viruses identified as human infectious agents, herpes simplex virus-1 (HSV-1)1 is the prototype of the ␣herpesvirus subfamily and of the family as a whole
There is evidence that it binds to the C terminus of the OBP and stimulates its helicase activity [5, 6], that it promotes the helicase activity of the viral helicase-primase complex (UL5-UL8-UL52) [7], and that it modulates the processivity of the viral polymerase (UL30) [8]
Summary
Viruses of the Herpesviridae family infect almost all vertebrates, including man, causing a variety of diseases. The crystal structure of a 60-residue C-terminal deletion construct of ICP8, the major single-stranded DNA-binding protein from herpes simplex virus-1, was determined at 3.0 Å resolution.
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