5vk3
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Apo ctPRC2 with E840A and K852D mutations in Ezh2== | |
| + | <StructureSection load='5vk3' size='340' side='right' caption='[[5vk3]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5vk3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VK3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VK3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bjs|5bjs]], [[5tqr|5tqr]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5vk3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vk3 OCA], [http://pdbe.org/5vk3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vk3 RCSB], [http://www.ebi.ac.uk/pdbsum/5vk3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vk3 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Polycomb-group proteins control many fundamental biological processes, such as anatomical development in mammals and vernalization in plants. Polycomb repressive complex 2 (PRC2) is responsible for methylation of histone H3 lysine 27 (H3K27), and trimethylated H3K27 (H3K27me3) is implicated in epigenetic gene silencing. Recent genomic, biochemical, and structural data indicate that PRC2 is broadly conserved from yeast to human in many aspects. Here, we determined the crystal structure of an apo PRC2 from the fungus Chaetomium thermophilum captured in a bona fide autoinhibited state, which represents a novel conformation of PRC2 associated with enzyme regulation in light of the basal and stimulated states that we reported previously. We found that binding by the cofactor SAM mitigates this autoinhibited structural state. Using steady-state enzyme kinetics, we also demonstrated that disrupting the autoinhibition results in a vastly activated enzyme complex. Autoinhibition provides a novel structural platform that may enable control of PRC2 activity in response to diverse transcriptional states and chromatin contexts and set a ground state to allow PRC2 activation by other cellular mechanisms as well. | ||
| - | + | Polycomb repressive complex 2 in an autoinhibited state.,Bratkowski M, Yang X, Liu X J Biol Chem. 2017 Jun 12. pii: jbc.M117.787572. doi: 10.1074/jbc.M117.787572. PMID:28607149<ref>PMID:28607149</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Bratkowski, M | + | <div class="pdbe-citations 5vk3" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bratkowski, M A]] | ||
[[Category: Liu, X]] | [[Category: Liu, X]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 11:41, 3 August 2017
Apo ctPRC2 with E840A and K852D mutations in Ezh2
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