7xd0: Difference between revisions
New page: '''Unreleased structure''' The entry 7xd0 is ON HOLD Authors: Ai, H.S., Liu, A.J., Lou, Z.Y., Liu, L. Description: cryo-EM structure of H2BK34ub nucleosome [[Category: Unreleased Struc... |
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==cryo-EM structure of H2BK34ub nucleosome== | |||
<StructureSection load='7xd0' size='340' side='right'caption='[[7xd0]], [[Resolution|resolution]] 3.48Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7xd0]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XD0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XD0 FirstGlance]. <br> | |||
</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=7xd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xd0 OCA], [https://pdbe.org/7xd0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xd0 RCSB], [https://www.ebi.ac.uk/pdbsum/7xd0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xd0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/A0A672PXK1_SINGR A0A672PXK1_SINGR]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.[ARBA:ARBA00002001][RuleBase:RU000528] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ubiquitination-dependent histone crosstalk plays critical roles in chromatin-associated processes and is highly associated with human diseases. Mechanism studies of the crosstalk have been of the central focus. Here our study on the crosstalk between H2BK34ub and Dot1L-catalyzed H3K79me suggests a novel mechanism of ubiquitination-induced nucleosome distortion to stimulate the activity of an enzyme. We determined the cryo-electron microscopy structures of Dot1L-H2BK34ub nucleosome complex and the H2BK34ub nucleosome alone. The structures reveal that H2BK34ub induces an almost identical orientation and binding pattern of Dot1L on nucleosome as H2BK120ub, which positions Dot1L for the productive conformation through direct ubiquitin-enzyme contacts. However, H2BK34-anchored ubiquitin does not directly interact with Dot1L as occurs in the case of H2BK120ub, but rather induces DNA and histone distortion around the modified site. Our findings establish the structural framework for understanding the H2BK34ub-H3K79me trans-crosstalk and highlight the diversity of mechanisms for histone ubiquitination to activate chromatin-modifying enzymes. | |||
H2B Lys34 Ubiquitination Induces Nucleosome Distortion to Stimulate Dot1L Activity.,Ai H, Sun M, Liu A, Sun Z, Liu T, Cao L, Liang L, Qu Q, Li Z, Deng Z, Tong Z, Chu G, Tian X, Deng H, Zhao S, Li JB, Lou Z, Liu L Nat Chem Biol. 2022 Sep;18(9):972-980. doi: 10.1038/s41589-022-01067-7. Epub 2022, Jun 23. PMID:35739357<ref>PMID:35739357</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7xd0" style="background-color:#fffaf0;"></div> | ||
[[Category: Liu | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Ai HS]] | |||
[[Category: Liu AJ]] | |||
[[Category: Liu L]] | |||
[[Category: Lou ZY]] | |||