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| | ==Crystal structure of the yeast COMPASS catalytic module== | | ==Crystal structure of the yeast COMPASS catalytic module== |
| - | <StructureSection load='6chg' size='340' side='right' caption='[[6chg]], [[Resolution|resolution]] 2.98Å' scene=''> | + | <StructureSection load='6chg' size='340' side='right'caption='[[6chg]], [[Resolution|resolution]] 2.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6chg]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_sphaerica Candida sphaerica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CHG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CHG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6chg]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Kluyveromyces_lactis_NRRL_Y-1140 Kluyveromyces lactis NRRL Y-1140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CHG FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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]] 2.985Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KLLA0_E24487g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica]), KLLA0_C10945g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica]), SET1, KLLA0F24134g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica]), KLLA0_A08800g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica]), KLLA0_E03521g ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=284590 Candida sphaerica])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6chg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6chg OCA], [https://pdbe.org/6chg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6chg RCSB], [https://www.ebi.ac.uk/pdbsum/6chg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6chg 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=6chg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6chg OCA], [http://pdbe.org/6chg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6chg RCSB], [http://www.ebi.ac.uk/pdbsum/6chg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6chg ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SET1_KLULA SET1_KLULA]] 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. | + | [https://www.uniprot.org/uniprot/Q6CLY5_KLULA Q6CLY5_KLULA] |
| | <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: Candida sphaerica]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Histone-lysine N-methyltransferase]] | + | [[Category: Kluyveromyces lactis NRRL Y-1140]] |
| - | [[Category: Hsu, P L]] | + | [[Category: Large Structures]] |
| - | [[Category: Li, H]] | + | [[Category: Hsu PL]] |
| - | [[Category: Zheng, N]] | + | [[Category: Li H]] |
| - | [[Category: Complex]] | + | [[Category: Zheng N]] |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Histone]]
| + | |
| - | [[Category: S-adenosylmethionine]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q6CLY5_KLULA
Publication Abstract from PubMed
The SET1/MLL family of histone methyltransferases is conserved in eukaryotes and regulates transcription by catalyzing histone H3K4 mono-, di-, and tri-methylation. These enzymes form a common five-subunit catalytic core whose assembly is critical for their basal and regulated enzymatic activities through unknown mechanisms. Here, we present the crystal structure of the intact yeast COMPASS histone methyltransferase catalytic module consisting of Swd1, Swd3, Bre2, Sdc1, and Set1. The complex is organized by Swd1, whose conserved C-terminal tail not only nucleates Swd3 and a Bre2-Sdc1 subcomplex, but also joins Set1 to construct a regulatory pocket next to the catalytic site. This inter-subunit pocket is targeted by a previously unrecognized enzyme-modulating motif in Swd3 and features a doorstop-style mechanism dictating substrate selectivity among SET1/MLL family members. By spatially mapping the functional components of COMPASS, our results provide a structural framework for understanding the multifaceted functions and regulation of the H3K4 methyltransferase family.
Crystal Structure of the COMPASS H3K4 Methyltransferase Catalytic Module.,Hsu PL, Li H, Lau HT, Leonen C, Dhall A, Ong SE, Chatterjee C, Zheng N Cell. 2018 Aug 23;174(5):1106-1116.e9. doi: 10.1016/j.cell.2018.06.038. Epub 2018, Aug 9. PMID:30100181[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hsu PL, Li H, Lau HT, Leonen C, Dhall A, Ong SE, Chatterjee C, Zheng N. Crystal Structure of the COMPASS H3K4 Methyltransferase Catalytic Module. Cell. 2018 Aug 23;174(5):1106-1116.e9. doi: 10.1016/j.cell.2018.06.038. Epub 2018, Aug 9. PMID:30100181 doi:http://dx.doi.org/10.1016/j.cell.2018.06.038
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