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

Citation:
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.
PDB ID: 1VHIDownload
MMDB ID: 51790
PDB Deposition Date: 1996/10/5
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 2.5  Å
Source Organism:
Similar Structures:
Biological Unit for 1VHI: dimeric; determined by author and by software (PISA)
Molecular Components in 1VHI
Label Count Molecule
Proteins (2 molecules)
2
Epstein Barr Virus Nuclear Antigen-1(Gene symbol: EBNA-1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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