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| | <StructureSection load='6e29' size='340' side='right'caption='[[6e29]], [[Resolution|resolution]] 1.82Å' scene=''> | | <StructureSection load='6e29' size='340' side='right'caption='[[6e29]], [[Resolution|resolution]] 1.82Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6e29]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cbs_117.65 Cbs 117.65]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E29 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E29 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e29]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus Thermothelomyces thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E29 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYCTH_2294520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=78579 CBS 117.65])</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]] 1.818Å</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=6e29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e29 OCA], [http://pdbe.org/6e29 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e29 RCSB], [http://www.ebi.ac.uk/pdbsum/6e29 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e29 ProSAT]</span></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=6e29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e29 OCA], [https://pdbe.org/6e29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e29 RCSB], [https://www.ebi.ac.uk/pdbsum/6e29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e29 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G2Q1Q9_MYCTT G2Q1Q9_MYCTT] |
| | <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: Cbs 117 65]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brunzelle, J S]] | + | [[Category: Thermothelomyces thermophilus]] |
| - | [[Category: Couture, J F]] | + | [[Category: Brunzelle JS]] |
| - | [[Category: Joshi, M]] | + | [[Category: Couture JF]] |
| - | [[Category: Yang, Y]] | + | [[Category: Joshi M]] |
| - | [[Category: Compass]] | + | [[Category: Yang Y]] |
| - | [[Category: Epigenetic]]
| + | |
| - | [[Category: Histone]]
| + | |
| - | [[Category: Histone h3 lys-4 methylation]]
| + | |
| - | [[Category: Mll1]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Set1]]
| + | |
| Structural highlights
Function
G2Q1Q9_MYCTT
Publication Abstract from PubMed
The methylation of histone 3 lysine 4 (H3K4) is carried out by an evolutionarily conserved family of methyltransferases referred to as complex of proteins associated with Set1 (COMPASS). The activity of the catalytic SET domain (su(var)3-9, enhancer-of-zeste, and trithorax) is endowed through forming a complex with a set of core proteins that are widely shared from yeast to humans. We obtained cryo-electron microscopy (cryo-EM) maps of the yeast Set1/COMPASS core complex at overall 4.0- to 4.4-A resolution, providing insights into its structural organization and conformational dynamics. The Cps50 C-terminal tail weaves within the complex to provide a central scaffold for assembly. The SET domain, snugly positioned at the junction of the Y-shaped complex, is extensively contacted by Cps60 (Bre2), Cps50 (Swd1), and Cps30 (Swd3). The mobile SET-I motif of the SET domain is engaged by Cps30, explaining its key role in COMPASS catalytic activity toward higher H3K4 methylation states.
Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex.,Qu Q, Takahashi YH, Yang Y, Hu H, Zhang Y, Brunzelle JS, Couture JF, Shilatifard A, Skiniotis G Cell. 2018 Aug 23;174(5):1117-1126.e12. doi: 10.1016/j.cell.2018.07.020. Epub, 2018 Aug 9. PMID:30100186[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qu Q, Takahashi YH, Yang Y, Hu H, Zhang Y, Brunzelle JS, Couture JF, Shilatifard A, Skiniotis G. Structure and Conformational Dynamics of a COMPASS Histone H3K4 Methyltransferase Complex. Cell. 2018 Aug 23;174(5):1117-1126.e12. doi: 10.1016/j.cell.2018.07.020. Epub, 2018 Aug 9. PMID:30100186 doi:http://dx.doi.org/10.1016/j.cell.2018.07.020
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