7VCL
structure of viral protein BKRF4 in complex with H2A-H2B
Summary for 7VCL
| Entry DOI | 10.2210/pdb7vcl/pdb |
| Descriptor | histone H2A-H2B, Tegument protein BKRF4 (2 entities in total) |
| Functional Keywords | h2a-h2b, h3-h4, histone, viral protein, nucleosome, nuclear protein |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 2 |
| Total formula weight | 29816.99 |
| Authors | Liu, Y.R. (deposition date: 2021-09-03, release date: 2022-08-03, Last modification date: 2023-11-29) |
| Primary citation | Liu, Y.,Li, Y.,Bao, H.,Liu, Y.,Chen, L.,Huang, H. Epstein-Barr Virus Tegument Protein BKRF4 is a Histone Chaperone. J.Mol.Biol., 434:167756-167756, 2022 Cited by PubMed Abstract: Histone chaperones, which constitute an interaction and functional network involved in all aspects of histone metabolism, have to date been identified only in eukaryotes. The Epstein-Barr virus tegument protein BKRF4 is a histone-binding protein that engages histones H2A-H2B and H3-H4, and cellular chromatin, inhibiting the host DNA damage response. Here, we identified BKRF4 as a bona fide viral histone chaperone whose histone-binding domain (HBD) forms a co-chaperone complex with the human histone chaperone ASF1 in vitro. We determined the crystal structures of the quaternary complex of the BKRF4 HBD with human H3-H4 dimer and the histone chaperone ASF1b and the ternary complex of the BKRF4 HBD with human H2A-H2B dimer. Through structural and biochemical studies, we elucidated the molecular basis for H3-H4 and H2A-H2B recognition by BKRF4. We also revealed two conserved motifs, D/EL and DEF/Y/W, within the BKRF4 HBD, which may represent common motifs through which histone chaperones target H3-H4 and H2A-H2B, respectively. In conclusion, our results identify BKRF4 as a histone chaperone encoded by the Epstein-Barr virus, representing a typical histone chaperone found in a non-eukaryote. We envision that more histone chaperones await identification and characterization in DNA viruses and even archaea. PubMed: 35870648DOI: 10.1016/j.jmb.2022.167756 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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