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| | ==Crystal structure of ATXR5 in complex with histone H3.1 and AdoHcy== | | ==Crystal structure of ATXR5 in complex with histone H3.1 and AdoHcy== |
| - | <StructureSection load='4o30' size='340' side='right' caption='[[4o30]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='4o30' size='340' side='right'caption='[[4o30]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o30]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Castor_bean Castor bean]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O30 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o30]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ricinus_communis Ricinus communis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O30 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RCOM_1460410 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3988 Castor bean])</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=4o30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o30 OCA], [https://pdbe.org/4o30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o30 RCSB], [https://www.ebi.ac.uk/pdbsum/4o30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o30 ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4o30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o30 OCA], [http://pdbe.org/4o30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o30 RCSB], [http://www.ebi.ac.uk/pdbsum/4o30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o30 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/ATXR5_RICCO ATXR5_RICCO] Histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). Has much higher activity on nucleosomes containing H3.1 than H3.3. Involved in the formation of constitutive heterochromatin and the silencing of heterochromatic elements (By similarity). |
| | <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: Castor bean]] | + | [[Category: Large Structures]] |
| - | [[Category: Histone-lysine N-methyltransferase]] | + | [[Category: Ricinus communis]] |
| - | [[Category: Bergamin, E]] | + | [[Category: Bergamin E]] |
| - | [[Category: Couture, J F]] | + | [[Category: Couture JF]] |
| - | [[Category: Mongeon, V]] | + | [[Category: Mongeon V]] |
| - | [[Category: Chromatin]]
| + | |
| - | [[Category: Epigenetic]]
| + | |
| - | [[Category: Histone h3]]
| + | |
| - | [[Category: Histone methylation]]
| + | |
| - | [[Category: Lysine methyltransferase]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Pcna]]
| + | |
| - | [[Category: Set domain]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Trithorax]]
| + | |
| Structural highlights
Function
ATXR5_RICCO Histone methyltransferase that specifically monomethylates 'Lys-37' of histone H3 (H3K27me1). Has much higher activity on nucleosomes containing H3.1 than H3.3. Involved in the formation of constitutive heterochromatin and the silencing of heterochromatic elements (By similarity).
Publication Abstract from PubMed
Histone variants have been proposed to act as determinants for posttranslational modifications with widespread regulatory functions. We identify a histone-modifying enzyme that selectively methylates the replication-dependent histone H3 variant H3.1. The crystal structure of the SET domain of the histone H3 lysine-27 (H3K27) methyltransferase ARABIDOPSIS TRITHORAX-RELATED PROTEIN 5 (ATXR5) in complex with a H3.1 peptide shows that ATXR5 contains a bipartite catalytic domain that specifically "reads" alanine-31 of H3.1. Variation at position 31 between H3.1 and replication-independent H3.3 is conserved in plants and animals, and threonine-31 in H3.3 is responsible for inhibiting the activity of ATXR5 and its paralog, ATXR6. Our results suggest a simple model for the mitotic inheritance of the heterochromatic mark H3K27me1 and the protection of H3.3-enriched genes against heterochromatization during DNA replication.
Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication.,Jacob Y, Bergamin E, Donoghue MT, Mongeon V, LeBlanc C, Voigt P, Underwood CJ, Brunzelle JS, Michaels SD, Reinberg D, Couture JF, Martienssen RA Science. 2014 Mar 14;343(6176):1249-53. doi: 10.1126/science.1248357. PMID:24626927[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jacob Y, Bergamin E, Donoghue MT, Mongeon V, LeBlanc C, Voigt P, Underwood CJ, Brunzelle JS, Michaels SD, Reinberg D, Couture JF, Martienssen RA. Selective methylation of histone H3 variant H3.1 regulates heterochromatin replication. Science. 2014 Mar 14;343(6176):1249-53. doi: 10.1126/science.1248357. PMID:24626927 doi:http://dx.doi.org/10.1126/science.1248357
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