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| | ==Structure of histone H3k4 methyltransferase== | | ==Structure of histone H3k4 methyltransferase== |
| - | <StructureSection load='6bx3' size='340' side='right' caption='[[6bx3]], [[Resolution|resolution]] 4.30Å' scene=''> | + | <SX load='6bx3' size='340' side='right' viewer='molstar' caption='[[6bx3]], [[Resolution|resolution]] 4.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6bx3]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BX3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BX3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6bx3]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_YJM789 Saccharomyces cerevisiae YJM789]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BX3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BX3 FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.3Å</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=6bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bx3 OCA], [http://pdbe.org/6bx3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bx3 RCSB], [http://www.ebi.ac.uk/pdbsum/6bx3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bx3 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=6bx3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bx3 OCA], [https://pdbe.org/6bx3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bx3 RCSB], [https://www.ebi.ac.uk/pdbsum/6bx3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bx3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SWD3_YEAST SWD3_YEAST]] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref> [[http://www.uniprot.org/uniprot/SPP1_YEAST SPP1_YEAST]] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref> [[http://www.uniprot.org/uniprot/A6ZT27_YEAS7 A6ZT27_YEAS7]] Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.[PIRNR:PIRNR037104] [[http://www.uniprot.org/uniprot/SDC1_YEAST SDC1_YEAST]] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently activates gene expression by regulating transcription elongation and plays a role in telomere length maintenance.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref> [[http://www.uniprot.org/uniprot/BRE2_YEAST BRE2_YEAST]] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref> [[http://www.uniprot.org/uniprot/SWD1_YEAST SWD1_YEAST]] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref> | + | [https://www.uniprot.org/uniprot/SPP1_YEAST SPP1_YEAST] The COMPASS (Set1C) complex specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.<ref>PMID:11742990</ref> <ref>PMID:11805083</ref> |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | 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.
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| - | 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<ref>PMID:30100186</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 6bx3" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Histone-lysine N-methyltransferase]] | + | [[Category: Large Structures]] |
| - | [[Category: Qu, Q H]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Skiniotis, G]] | + | [[Category: Saccharomyces cerevisiae YJM789]] |
| - | [[Category: Gene regulation-transferase complex]] | + | [[Category: Qu QH]] |
| - | [[Category: Histone h3k4 methyltransferase]] | + | [[Category: Skiniotis G]] |
