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| | <StructureSection load='5kjh' size='340' side='right'caption='[[5kjh]], [[Resolution|resolution]] 2.27Å' scene=''> | | <StructureSection load='5kjh' size='340' side='right'caption='[[5kjh]], [[Resolution|resolution]] 2.27Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5kjh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5ch1 5ch1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5KJH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5kjh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KJH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=759272 CHATD]), 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'>[https://proteopedia.org/fgij/fg.htm?mol=5kjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjh OCA], [https://pdbe.org/5kjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kjh RCSB], [https://www.ebi.ac.uk/pdbsum/5kjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjh ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5kjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kjh OCA], [http://pdbe.org/5kjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kjh RCSB], [http://www.ebi.ac.uk/pdbsum/5kjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kjh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EED_CHATD EED_CHATD] Component of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3) (PubMed:26472914, PubMed:29904056). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development (PubMed:26472914, PubMed:28008037, PubMed:28607149, PubMed:29904056). EED is not a catalytic subunit but is required for the complex regulation of histone H3 lysine methylation by EZH2 (PubMed:26472914, PubMed:28008037, PubMed:28607149, PubMed:29904056).<ref>PMID:26472914</ref> <ref>PMID:28008037</ref> <ref>PMID:28607149</ref> <ref>PMID:29904056</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jiao, L]] | + | [[Category: Jiao L]] |
| - | [[Category: Liu, X]] | + | [[Category: Liu X]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
EED_CHATD Component of the of the Polycomb Repressive Complex 2 (PRC2), a histone H3 lysine methyltransferase responsible for generating mono-, di-, and tri-methylation on Lys27 (H3K27me1, H3K27me2 and H3K27me3) (PubMed:26472914, PubMed:29904056). The tri-methylated form is known to be critical in gene repression, and its proper placement is essential in defining repression patterns during development (PubMed:26472914, PubMed:28008037, PubMed:28607149, PubMed:29904056). EED is not a catalytic subunit but is required for the complex regulation of histone H3 lysine methylation by EZH2 (PubMed:26472914, PubMed:28008037, PubMed:28607149, PubMed:29904056).[1] [2] [3] [4]
Publication Abstract from PubMed
Zhang et al suggested that in the crystal structure of a polycomb repressive complex 2 from Chaetomium thermophilum (ctPRC2), a flexible linker region, but not the H3K27M cancer mutant peptide, better fits the electron density. Based on our new data, we agree with this alternative interpretation and provide the crystal structure of ctPRC2 bound to a bona fide H3K27M sequence.
Response to Comment on "Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2".,Jiao L, Liu X Science. 2016 Dec 23;354(6319):1543. doi: 10.1126/science.aaj2335. PMID:28008038[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jiao L, Liu X. Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2. Science. 2015 Oct 16;350(6258):aac4383. PMID:26472914 doi:10.1126/science.aac4383
- ↑ Zhang Y, Justin N, Wilson JR, Gamblin SJ. Comment on "Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2". Science. 2016 Dec 23;354(6319):1543. doi: 10.1126/science.aaf6236. PMID:28008037 doi:http://dx.doi.org/10.1126/science.aaf6236
- ↑ Bratkowski M, Yang X, Liu X. Polycomb repressive complex 2 in an autoinhibited state. J Biol Chem. 2017 Jun 12. pii: jbc.M117.787572. doi: 10.1074/jbc.M117.787572. PMID:28607149 doi:http://dx.doi.org/10.1074/jbc.M117.787572
- ↑ Bratkowski M, Yang X, Liu X. An Evolutionarily Conserved Structural Platform for PRC2 Inhibition by a Class of Ezh2 Inhibitors. Sci Rep. 2018 Jun 14;8(1):9092. doi: 10.1038/s41598-018-27175-w. PMID:29904056 doi:http://dx.doi.org/10.1038/s41598-018-27175-w
- ↑ Jiao L, Liu X. Response to Comment on "Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2". Science. 2016 Dec 23;354(6319):1543. doi: 10.1126/science.aaj2335. PMID:28008038 doi:http://dx.doi.org/10.1126/science.aaj2335
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