1VHI

EPSTEIN BARR VIRUS NUCLEAR ANTIGEN-1 DNA-BINDING DOMAIN, RESIDUES 470-607

Summary for 1VHI

• Entry DOI: 10.2210/pdb1vhi/pdb
• Descriptor: EPSTEIN BARR VIRUS NUCLEAR ANTIGEN-1 (2 entities in total)
• Functional Keywords: nuclear protein, dna-binding, activator, origin-binding protein
• Biological source: Human herpesvirus 4 (Epstein-Barr virus)
• Cellular location: Host nucleus: P03211
• Total number of polymer chains: 2
• Total formula weight: 30727.46

Authors

Bochkarev, A.,Barwell, J.,Pfuetzner, R.,Furey, W.,Edwards, A.,Frappier, L. (deposition date: 1996-10-05, release date: 1996-12-23, Last modification date: 2024-02-14)

Primary citation

Bochkarev, A.,Barwell, J.A.,Pfuetzner, R.A.,Furey Jr., W.,Edwards, A.M.,Frappier, L.
Crystal structure of the DNA-binding domain of the Epstein-Barr virus origin-binding protein EBNA 1.
Cell(Cambridge,Mass.), 83:39-46, 1995

PubMed Abstract: The crystal structure of the DNA-binding and dimerization domains of the Epstein-Barr virus nuclear antigen 1 (EBNA1), which binds to and activates DNA replication from the latent origin of replication in Epstein-Barr virus, was solved at 2.5 A resolution. EBNA1 appears to bind DNA via two independent regions termed the core and the flanking DNA-binding domains. The core DNA-binding domain, which comprises both the dimerization domain and a helix predicted to bind the inner portion of the EBNA1 DNA recognition element, was remarkably similar to the structure of the papillomavirus E2 protein, despite a complete lack of sequence conservation. The flanking DNA-binding domain, only a portion of which is contained in the current structure, consists in part of an alpha helix whose N-terminus contacts the outer regions of the EBNA1 DNA recognition element.

PubMed: 7553871
DOI: 10.1016/0092-8674(95)90232-5

Experimental method

X-RAY DIFFRACTION (2.5 Å)