3m59 - Revision history

OCA at 08:48, 6 September 2023

OCA — Wed, 06 Sep 2023 08:48:27 GMT

←Older revision		Revision as of 08:48, 6 September 2023
Line 3:		Line 3:
	<StructureSection load='3m59' size='340' side='right'caption='[[3m59]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='3m59' size='340' side='right'caption='[[3m59]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M59 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M59 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 1.7Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=~~MLY~~:~~N-DIMETHYL-LYSINE~~'>~~MLY~~</scene><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b~~></td><~~td class~~=~~"sblockDat"><div style~~=~~'overflow~~: ~~auto; max~~-~~height: 3em;~~'>~~[[2f69\|2f69]], [[3m54\|3m54]], [[3m55\|3m55]], [[3m56\|3m56]], [[3m57\|3m57]], [[3m58\|3m58]], [[3m53\|3m53]], [[3m5a\|3m5a]]~~</~~div~~>~~</td></tr>~~	+
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA1717~~, ~~KMT7, SET7, SET9, SETD7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~<~~/td></tr>~~	+
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone~~-~~lysine_N~~-~~methyltransferase Histone~~-~~lysine N-methyltransferase], with EC number [https://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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [https://pdbe.org/3m59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [https://www.ebi.ac.uk/pdbsum/3m59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m59 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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [https://pdbe.org/3m59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [https://www.ebi.ac.uk/pdbsum/3m59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m59 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>	+	[https://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Histone-lysine N-methyltransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Brunzelle~~, J S~~]]	+	[[Category: Brunzelle JS]]
-	[[Category: Couture, J F]]	+	[[Category: Couture J-F]]
-	[[Category: ~~Dirk, L M~~]]	+	[[Category: Del Rizzo PA]]
-	[[Category: ~~Houtz, R L~~]]	+	[[Category: Dirk LM]]
-	[[Category: ~~Rizzo, P A.Del~~]]	+	[[Category: Houtz RL]]
-	[[Category: Roiko~~, M S~~]]	+	[[Category: Roiko MS]]
-	[[Category: Strunk~~, B S~~]]	+	[[Category: Strunk BS]]
-	[[Category: Trievel~~, R C]]~~	+	[[Category: Trievel RC]]
-	~~[[Category: Chromatin regulator]]~~	+
-	~~[[Category: Chromosomal protein]]~~	+
-	~~[[Category: Methyltransferase]]~~	+
-	~~[[Category: N-dimethyllysine]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: S-adenosyl-l-homocysteine]]~~	+
-	~~[[Category: S-adenosyl-l-methionine]]~~	+
-	~~[[Category: Set domain]]~~	+
-	~~[[Category: Taf10 peptide]]~~	+
-	~~[[Category: Ternary complex]]~~	+
-	~~[[Category: Transcription]]~~	+
-	~~[[Category: Transcription regulation]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:37, 6 October 2021

OCA — Wed, 06 Oct 2021 05:37:04 GMT

←Older revision		Revision as of 05:37, 6 October 2021
Line 1:		Line 1:

	==SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy==		==SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy==
-	<StructureSection load='3m59' size='340' side='right' caption='[[3m59]], [[Resolution\|resolution]] 1.70Å' scene=''>	+	<StructureSection load='3m59' size='340' side='right'caption='[[3m59]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m59]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3M59 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m59]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M59 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f69\|2f69]], [[3m54\|3m54]], [[3m55\|3m55]], [[3m56\|3m56]], [[3m57\|3m57]], [[3m58\|3m58]], [[3m53\|3m53]], [[3m5a\|3m5a]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2f69\|2f69]], [[3m54\|3m54]], [[3m55\|3m55]], [[3m56\|3m56]], [[3m57\|3m57]], [[3m58\|3m58]], [[3m53\|3m53]], [[3m5a\|3m5a]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA1717, KMT7, SET7, SET9, SETD7 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA1717, KMT7, SET7, SET9, SETD7 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [~~http~~://pdbe.org/3m59 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3m59 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3m59 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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [https://pdbe.org/3m59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [https://www.ebi.ac.uk/pdbsum/3m59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m59 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>	+	[[https://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/3m59_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/3m59_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3m59" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3m59" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 41:
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Brunzelle, J S]]		[[Category: Brunzelle, J S]]
	[[Category: Couture, J F]]		[[Category: Couture, J F]]

OCA at 08:04, 8 November 2017

OCA — Wed, 08 Nov 2017 08:04:58 GMT

←Older revision		Revision as of 08:04, 8 November 2017
Line 32:		Line 32:
	</div>		</div>
	<div class="pdbe-citations 3m59" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3m59" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Histone methyltransferase\|Histone methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:03, 5 August 2016

OCA — Fri, 05 Aug 2016 18:03:37 GMT

←Older revision		Revision as of 18:03, 5 August 2016
Line 1:		Line 1:
		+
	==SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy==		==SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy==
	<StructureSection load='3m59' size='340' side='right' caption='[[3m59]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='3m59' size='340' side='right' caption='[[3m59]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3m59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M59 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3m59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M59 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f69\|2f69]], [[3m54\|3m54]], [[3m55\|3m55]], [[3m56\|3m56]], [[3m57\|3m57]], [[3m58\|3m58]], [[3m53\|3m53]], [[3m5a\|3m5a]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f69\|2f69]], [[3m54\|3m54]], [[3m55\|3m55]], [[3m56\|3m56]], [[3m57\|3m57]], [[3m58\|3m58]], [[3m53\|3m53]], [[3m5a\|3m5a]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA1717, KMT7, SET7, SET9, SETD7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA1717, KMT7, SET7, SET9, SETD7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [http://www.ebi.ac.uk/pdbsum/3m59 PDBsum]</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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [http://pdbe.org/3m59 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [http://www.ebi.ac.uk/pdbsum/3m59 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3m59 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 20:		Line 21:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3m59 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 30:		Line 31:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3m59" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 38:		Line 40:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Brunzelle, J S]]		[[Category: Brunzelle, J S]]
	[[Category: Couture, J F]]		[[Category: Couture, J F]]

OCA at 04:40, 25 December 2014

OCA — Thu, 25 Dec 2014 04:40:14 GMT

←Older revision		Revision as of 04:40, 25 December 2014
Line 10:		Line 10:
	<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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [http://www.ebi.ac.uk/pdbsum/3m59 PDBsum]</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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [http://www.ebi.ac.uk/pdbsum/3m59 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SETD7_HUMAN SETD7_HUMAN]] Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.<ref>PMID:12588998</ref> <ref>PMID:15099517</ref> <ref>PMID:16141209</ref> <ref>PMID:17108971</ref> <ref>PMID:12540855</ref> <ref>PMID:15525938</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 09:58, 9 December 2014

OCA — Tue, 09 Dec 2014 09:58:11 GMT

←Older revision		Revision as of 09:58, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3m59.~~png~~\|~~left~~\|200px]]	+	==SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy==
		+	<StructureSection load='3m59' size='340' side='right' caption='[[3m59]], [[Resolution\|resolution]] 1.70Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3m59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3M59 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2f69\|2f69]], [[3m54\|3m54]], [[3m55\|3m55]], [[3m56\|3m56]], [[3m57\|3m57]], [[3m58\|3m58]], [[3m53\|3m53]], [[3m5a\|3m5a]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">KIAA1717, KMT7, SET7, SET9, SETD7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3m59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m59 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3m59 RCSB], [http://www.ebi.ac.uk/pdbsum/3m59 PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m5/3m59_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	SET domain lysine methyltransferases (KMTs) methylate specific lysine residues in histone and non-histone substrates. These enzymes also display product specificity by catalyzing distinct degrees of methylation of the lysine epsilon-amino group. To elucidate the molecular mechanism underlying this specificity, we have characterized the Y245A and Y305F mutants of the human KMT SET7/9 (also known as KMT7) that alter its product specificity from a monomethyltransferase to a di- and a trimethyltransferase, respectively. Crystal structures of these mutants in complex with peptides bearing unmodified, mono-, di-, and trimethylated lysines illustrate the roles of active site water molecules in aligning the lysine epsilon-amino group for methyl transfer with S-adenosylmethionine. Displacement or dissociation of these solvent molecules enlarges the diameter of the active site, accommodating the increasing size of the methylated epsilon-amino group during successive methyl transfer reactions. Together, these results furnish new insights into the roles of active site water molecules in modulating lysine multiple methylation by SET domain KMTs and provide the first molecular snapshots of the mono-, di-, and trimethyl transfer reactions catalyzed by these enzymes.

-	~~{{STRUCTURE_3m59\| PDB=3m59 \| SCENE= }}~~	+	SET7/9 catalytic mutants reveal the role of active site water molecules in lysine multiple methylation.,Del Rizzo PA, Couture JF, Dirk LM, Strunk BS, Roiko MS, Brunzelle JS, Houtz RL, Trievel RC J Biol Chem. 2010 Oct 8;285(41):31849-58. Epub 2010 Aug 1. PMID:20675860<ref>PMID:20675860</ref>

-	~~===SET7~~/~~9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-		+	==See Also==
-	==~~About this Structure~~==	+	*[[Histone methyltransferase\|Histone methyltransferase]]
-	[[~~3m59~~]] ~~is a 2 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA].~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Brunzelle, J S.]]	+	[[Category: Brunzelle, J S]]
-	[[Category: Couture, J F.]]	+	[[Category: Couture, J F]]
-	[[Category: Dirk, L M.]]	+	[[Category: Dirk, L M]]
-	[[Category: Houtz, R L.]]	+	[[Category: Houtz, R L]]
-	[[Category: Rizzo, P A.Del.]]	+	[[Category: Rizzo, P A.Del]]
-	[[Category: Roiko, M S.]]	+	[[Category: Roiko, M S]]
-	[[Category: Strunk, B S.]]	+	[[Category: Strunk, B S]]
-	[[Category: Trievel, R C.]]	+	[[Category: Trievel, R C]]
	[[Category: Chromatin regulator]]		[[Category: Chromatin regulator]]
	[[Category: Chromosomal protein]]		[[Category: Chromosomal protein]]

OCA: Protected "3m59" [edit=sysop:move=sysop]

OCA — Wed, 14 Nov 2012 06:42:06 GMT

Protected "3m59" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:42, 14 November 2012

OCA at 06:42, 14 November 2012

OCA — Wed, 14 Nov 2012 06:42:02 GMT

←Older revision		Revision as of 06:42, 14 November 2012
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3m59.png\|left\|200px]]
-	[[Image:3m59.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3m59", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3m59\| PDB=3m59 \| SCENE= }}		{{STRUCTURE_3m59\| PDB=3m59 \| SCENE= }}

Line 14:		Line 7:

	==About this Structure==		==About this Structure==
-	~~3M59~~ is a 2 ~~chains~~ structure with ~~sequences~~ from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA].	+	[[3m59]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA].
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 38:		Line 31:
	[[Category: Transcription regulation]]		[[Category: Transcription regulation]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:38:01 2010''

OCA at 08:31, 28 July 2010

OCA — Wed, 28 Jul 2010 08:31:21 GMT

←Older revision		Revision as of 08:31, 28 July 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3m59.jpg\|left\|200px]]

-	The ~~entry 3m59~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3m59", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3m59\| PDB=3m59 \| SCENE= }}

-	~~Authors: Del Rizzo, P.A., Couture, J.~~-~~F., Roiko, M.S., Strunk, B.S., Brunzelle, J.S., Dirk, L.M., Houtz, R.L., Trievel, R.C.~~	+	===SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy===

-	Description: SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Apr 21 09~~:35:41 2010''	+	==About this Structure==
		+	3M59 is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M59 OCA].
		+	[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Brunzelle, J S.]]
		+	[[Category: Couture, J F.]]
		+	[[Category: Dirk, L M.]]
		+	[[Category: Houtz, R L.]]
		+	[[Category: Rizzo, P A.Del.]]
		+	[[Category: Roiko, M S.]]
		+	[[Category: Strunk, B S.]]
		+	[[Category: Trievel, R C.]]
		+	[[Category: Chromatin regulator]]
		+	[[Category: Chromosomal protein]]
		+	[[Category: Methyltransferase]]
		+	[[Category: N-dimethyllysine]]
		+	[[Category: Nucleus]]
		+	[[Category: S-adenosyl-l-homocysteine]]
		+	[[Category: S-adenosyl-l-methionine]]
		+	[[Category: Set domain]]
		+	[[Category: Taf10 peptide]]
		+	[[Category: Ternary complex]]
		+	[[Category: Transcription]]
		+	[[Category: Transcription regulation]]
		+	[[Category: Transferase]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 28 12:38:01 2010''

OCA at 06:35, 21 April 2010

OCA — Wed, 21 Apr 2010 06:35:42 GMT

←Older revision		Revision as of 06:35, 21 April 2010
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3m59 is ON HOLD	+	The entry 3m59 is ON HOLD until Paper Publication

	Authors: Del Rizzo, P.A., Couture, J.-F., Roiko, M.S., Strunk, B.S., Brunzelle, J.S., Dirk, L.M., Houtz, R.L., Trievel, R.C.		Authors: Del Rizzo, P.A., Couture, J.-F., Roiko, M.S., Strunk, B.S., Brunzelle, J.S., Dirk, L.M., Houtz, R.L., Trievel, R.C.
Line 7:		Line 7:
	Description: SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy		Description: SET7/9 Y245A in complex with TAF10-K189me2 peptide and AdoHcy

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 14 09:21:41 2010''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 21 09:35:41 2010''