View source for 7vcq


==structure of viral protein BKRF4 in complex with H3.3-H4-ASF1==
<StructureSection load='7vcq' size='340' side='right'caption='[[7vcq]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7vcq]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Epstein-barr_virus_strain_ag876 Epstein-barr virus strain ag876] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VCQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VCQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7vcq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vcq OCA], [https://pdbe.org/7vcq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vcq RCSB], [https://www.ebi.ac.uk/pdbsum/7vcq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vcq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H33_HUMAN H33_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Epstein-Barr Virus Tegument Protein BKRF4 is a Histone Chaperone.,Liu Y, Li Y, Bao H, Liu Y, Chen L, Huang H J Mol Biol. 2022 Jul 21;434(19):167756. doi: 10.1016/j.jmb.2022.167756. PMID:35870648<ref>PMID:35870648</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7vcq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
*[[Histone 3D structures|Histone 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Epstein-barr virus strain ag876]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Liu YR]]