1urj

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SINGLE STRANDED DNA-BINDING PROTEIN(ICP8) FROM HERPES SIMPLEX VIRUS-1SINGLE STRANDED DNA-BINDING PROTEIN(ICP8) FROM HERPES SIMPLEX VIRUS-1

Structural highlights

1urj is a 2 chain structure with sequence from Human herpesvirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding.,Mapelli M, Panjikar S, Tucker PA J Biol Chem. 2005 Jan 28;280(4):2990-7. Epub 2004 Oct 26. PMID:15507432[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Mapelli M, Panjikar S, Tucker PA. The crystal structure of the herpes simplex virus 1 ssDNA-binding protein suggests the structural basis for flexible, cooperative single-stranded DNA binding. J Biol Chem. 2005 Jan 28;280(4):2990-7. Epub 2004 Oct 26. PMID:15507432 doi:10.1074/jbc.M406780200

1urj, resolution 3.00Å

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