5KDM: Crystal structure of EBV tegument protein BNRF1 in complex with histone chaperone DAXX and histones H3.3-H4

The histone H3.3 chaperone DAXX is implicated in formation of heterochromatin and transcription silencing, especially for newly infecting DNA virus genomes entering the nucleus. Epstein-Barr virus (EBV) can efficiently establish stable latent infection as a chromatinized episome in the nucleus of infected cells. The EBV tegument BNRF1 is a DAXX-interacting protein required for the establishment of selective viral gene expression during latency. Here we report the structure of BNRF1 DAXX-interaction domain (DID) in complex with DAXX histone-binding domain (HBD) and histones H3.3-H4. BNRF1 DID contacts DAXX HBD and histones through non-conserved loops. The BNRF1-DAXX interface is responsible for BNRF1 localization to PML-nuclear bodies typically associated with host-antiviral resistance and transcriptional repression. Paradoxically, the interface is also required for selective transcription activation of viral latent cycle genes required for driving B-cell proliferation. These findings reveal molecular details of virus reprogramming of an antiviral histone chaperone to promote viral latency and cellular immortalization.
PDB ID: 5KDMDownload
MMDB ID: 142859
PDB Deposition Date: 2016/6/8
Updated in MMDB: 2016/09
Experimental Method:
x-ray diffraction
Resolution: 3.5  Å
Source Organism:
Epstein-barr virus strain ag876
Similar Structures:
Biological Unit for 5KDM: tetrameric; determined by author
Molecular Components in 5KDM
Label Count Molecule
Proteins (4 molecules)
Histone H3.3(Gene symbol: H3F3A)
Molecule annotation
Histone H4(Gene symbol: HIST1H4I)
Molecule annotation
Death Domain-associated Protein 6(Gene symbol: DAXX)
Molecule annotation
Major Tegument Protein(Gene symbol: HHV4tp2_gp03)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB