7vcl: Difference between revisions
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New page: '''Unreleased structure''' The entry 7vcl is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==structure of viral protein BKRF4 in complex with H2A-H2B== | ||
<StructureSection load='7vcl' size='340' side='right'caption='[[7vcl]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7vcl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7VCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VCL 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]] 3.2Å</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=7vcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vcl OCA], [https://pdbe.org/7vcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vcl RCSB], [https://www.ebi.ac.uk/pdbsum/7vcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vcl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BKRF4_EBVG BKRF4_EBVG] | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7vcl" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Histone 3D structures|Histone 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Human gammaherpesvirus 4]] | |||
[[Category: Large Structures]] | |||
[[Category: Liu YR]] | |||
Latest revision as of 17:23, 29 November 2023
structure of viral protein BKRF4 in complex with H2A-H2B
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