5KDM

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

Summary for 5KDM

• Entry DOI: 10.2210/pdb5kdm/pdb
• Descriptor: Histone H3.3, Histone H4, Death domain-associated protein 6, ... (4 entities in total)
• Functional Keywords: histone chaperone, gene repression, chaperone - dna binding protein complex, chaperone / dna binding protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus: P84243 P62805; Cytoplasm . Isoform beta: Nucleus . Isoform gamma: Nucleus : Q9UER7; Virion tegument : Q1HVJ0
• Total number of polymer chains: 4
• Total formula weight: 74632.84

Authors

Huang, H.,Patel, D. (deposition date: 2016-06-08, release date: 2016-09-07, Last modification date: 2023-09-27)

Primary citation

Huang, H.,Deng, Z.,Vladimirova, O.,Wiedmer, A.,Lu, F.,Lieberman, P.M.,Patel, D.J.
Structural basis underlying viral hijacking of a histone chaperone complex.
Nat Commun, 7:12707-12707, 2016

PubMed Abstract: 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.

PubMed: 27581705
DOI: 10.1038/ncomms12707

Experimental method

X-RAY DIFFRACTION (3.5 Å)