5bjs: Difference between revisions
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<StructureSection load='5bjs' size='340' side='right' caption='[[5bjs]], [[Resolution|resolution]] 2.19Å' scene=''> | <StructureSection load='5bjs' size='340' side='right' caption='[[5bjs]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5bjs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BJS FirstGlance]. <br> | <table><tr><td colspan='2'>[[5bjs]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_144.50 Cbs 144.50] and [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BJS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BJS 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> | </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">[[5tqr|5tqr]], [[5tqt|5tqt]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tqr|5tqr]], [[5tqt|5tqt]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0029920 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=209285 CBS 144.50]), CTHT_0006210 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</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=5bjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bjs OCA], [http://pdbe.org/5bjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bjs RCSB], [http://www.ebi.ac.uk/pdbsum/5bjs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bjs ProSAT]</span></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=5bjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bjs OCA], [http://pdbe.org/5bjs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bjs RCSB], [http://www.ebi.ac.uk/pdbsum/5bjs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bjs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cbs 144 50]] | |||
[[Category: Chatd]] | |||
[[Category: Bratkowski, M A]] | [[Category: Bratkowski, M A]] | ||
[[Category: Liu, X]] | [[Category: Liu, X]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 15:23, 6 November 2017
Apo ctPRC2 in an autoinhibited stateApo ctPRC2 in an autoinhibited state
Structural highlights
Publication Abstract from PubMedPolycomb-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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