8ieg: Difference between revisions

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'''Unreleased structure'''


The entry 8ieg is ON HOLD  until Paper Publication
==Bre1(mRBD-RING)/Rad6-Ub/nucleosome complex==
<StructureSection load='8ieg' size='340' side='right'caption='[[8ieg]], [[Resolution|resolution]] 3.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ieg]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8IEG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IEG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.44&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=8ieg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ieg OCA], [https://pdbe.org/8ieg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ieg RCSB], [https://www.ebi.ac.uk/pdbsum/8ieg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ieg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BRE1_YEAST BRE1_YEAST] E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H2B to form H2BK123ub1 in association with the E2 enzyme RAD6/UBC2. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. It thereby plays a central role in histone code and gene regulation. Also modulates the formation of double-strand breaks during meiosis.<ref>PMID:12535538</ref> <ref>PMID:12535539</ref> <ref>PMID:12876294</ref> <ref>PMID:15280549</ref> <ref>PMID:15632065</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histone H2B monoubiquitylation plays essential roles in chromatin-based transcriptional processes. A RING-type E3 ligase (yeast Bre1 or human RNF20/RNF40) and an E2 ubiquitin-conjugating enzyme (yeast Rad6 or human hRAD6A), together, precisely deposit ubiquitin on H2B K123 in yeast or K120 in humans. Here, we developed a chemical trapping strategy and successfully captured the transient structures of Bre1- or RNF20/RNF40-mediated ubiquitin transfer from Rad6 or hRAD6A to nucleosomal H2B. Our structures show that Bre1 and RNF40 directly bind nucleosomal DNA, exhibiting a conserved E3/E2/nucleosome interaction pattern from yeast to humans for H2B monoubiquitylation. We also find an uncanonical non-hydrophobic contact in the Bre1 RING-Rad6 interface, which positions Rad6 directly above the target H2B lysine residue. Our study provides mechanistic insights into the site-specific monoubiquitylation of H2B, reveals a critical role of nucleosomal DNA in mediating E3 ligase recognition, and provides a framework for understanding the cancer-driving mutations of RNF20/RNF40.


Authors:  
Mechanistic insights into nucleosomal H2B monoubiquitylation mediated by yeast Bre1-Rad6 and its human homolog RNF20/RNF40-hRAD6A.,Deng Z, Ai H, Sun M, Tong Z, Du Y, Qu Q, Zhang L, Xu Z, Tao S, Shi Q, Li JB, Pan M, Liu L Mol Cell. 2023 Aug 17:S1097-2765(23)00607-X. doi: 10.1016/j.molcel.2023.08.001. PMID:37633270<ref>PMID:37633270</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8ieg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Ai H]]
[[Category: Deng Z]]
[[Category: Liu L]]
[[Category: Pan M]]
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