7VCL

structure of viral protein BKRF4 in complex with H2A-H2B

7VCL の概要

• エントリーDOI: 10.2210/pdb7vcl/pdb
• 分子名称: histone H2A-H2B, Tegument protein BKRF4 (2 entities in total)
• 機能のキーワード: h2a-h2b, h3-h4, histone, viral protein, nucleosome, nuclear protein
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29816.99

構造登録者

Liu, Y.R. (登録日: 2021-09-03, 公開日: 2022-08-03, 最終更新日: 2023-11-29)

主引用文献

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

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: 35870648
DOI: 10.1016/j.jmb.2022.167756

実験手法

X-RAY DIFFRACTION (3.2 Å)