4qep - Revision history

OCA at 17:31, 20 September 2023

OCA — Wed, 20 Sep 2023 17:31:15 GMT

←Older revision		Revision as of 17:31, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QEP FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QEP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 3.1Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [https://pdbe.org/4qep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [https://www.ebi.ac.uk/pdbsum/4qep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep 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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [https://pdbe.org/4qep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [https://www.ebi.ac.uk/pdbsum/4qep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep ProSAT]</span></td></tr>
	</table>		</table>

OCA at 11:26, 15 February 2023

OCA — Wed, 15 Feb 2023 11:26:18 GMT

←Older revision		Revision as of 11:26, 15 February 2023
Line 3:		Line 3:
	<StructureSection load='4qep' size='340' side='right'caption='[[4qep]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='4qep' size='340' side='right'caption='[[4qep]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Arath Arath~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4QEP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QEP FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"~~><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr~~ id~~='NonStdRes'><td class~~="~~sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat~~"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene><~~/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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [https://pdbe.org/4qep PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [https://www.ebi.ac.uk/pdbsum/4qep PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep ProSAT]</span></td></tr>
-	~~<tr id~~='~~related'><td class~~=~~"sblockLbl"><b>[[Related_structure\|Related~~:~~]]</b></td><td class="sblockDat">[[4qen\|4qen]], [[4qeo\|4qeo]]</td></tr>~~	+
-	~~<tr id='gene~~'>~~<td class="sblockLbl"><b>[[Gene\|Gene:]]~~</~~b></td><td class="sblockDat"~~>~~SUVH4~~, ~~KYP, SDG33, SET33, At5g13960, MAC12.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])~~<~~/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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [~~http~~://pdbe.org/4qep PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4qep PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/SUVH4_ARATH SUVH4_ARATH]] Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. The silencing mechanism via DNA CpNpG methylation requires the targeting of chromomethylase CMT3 to methylated histones, probably through an interaction with an HP1-like adapter. By its function, KYP is directly required for the maintenance of the DNA CpNpG and asymmetric methylation. Involved in the silencing of transposable elements.<ref>PMID:11898023</ref> <ref>PMID:15457214</ref> <ref>PMID:15598823</ref> <ref>PMID:16277745</ref> <ref>PMID:16287862</ref>	+	[https://www.uniprot.org/uniprot/SUVH4_ARATH SUVH4_ARATH] Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. The silencing mechanism via DNA CpNpG methylation requires the targeting of chromomethylase CMT3 to methylated histones, probably through an interaction with an HP1-like adapter. By its function, KYP is directly required for the maintenance of the DNA CpNpG and asymmetric methylation. Involved in the silencing of transposable elements.<ref>PMID:11898023</ref> <ref>PMID:15457214</ref> <ref>PMID:15598823</ref> <ref>PMID:16277745</ref> <ref>PMID:16287862</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 20:

	==See Also==		==See Also==
-	*[[Histone methyltransferase\|Histone methyltransferase]]	+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Arath]]~~	+	[[Category: Arabidopsis thaliana]]
-	~~[[Category: Histone-lysine N-methyltransferase~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Du, J]]	+	[[Category: Du J]]
-	[[Category: Li, S]]	+	[[Category: Li S]]
-	[[Category: Patel~~, D J]]~~	+	[[Category: Patel DJ]]
-	~~[[Category: Histone methylation]]~~	+
-	~~[[Category: Methylated dna]]~~	+
-	~~[[Category: Methylation]]~~	+
-	~~[[Category: Set]]~~	+
-	~~[[Category: Sra]]~~	+
-	~~[[Category: Transcription-dna complex~~]]	+

OCA at 09:16, 24 April 2019

OCA — Wed, 24 Apr 2019 09:16:41 GMT

←Older revision		Revision as of 09:16, 24 April 2019
Line 1:		Line 1:

	==crystal structure of KRYPTONITE in complex with mCHG DNA and SAH==		==crystal structure of KRYPTONITE in complex with mCHG DNA and SAH==
-	<StructureSection load='4qep' size='340' side='right' caption='[[4qep]], [[Resolution\|resolution]] 3.10Å' scene=''>	+	<StructureSection load='4qep' size='340' side='right'caption='[[4qep]], [[Resolution\|resolution]] 3.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QEP FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QEP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4qen\|4qen]], [[4qeo\|4qeo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4qen\|4qen]], [[4qeo\|4qeo]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SUVH4, KYP, SDG33, SET33, At5g13960, MAC12.7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [http://pdbe.org/4qep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [http://www.ebi.ac.uk/pdbsum/4qep PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep 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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [http://pdbe.org/4qep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [http://www.ebi.ac.uk/pdbsum/4qep PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep ProSAT]</span></td></tr>
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	</div>		</div>
	<div class="pdbe-citations 4qep" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4qep" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone methyltransferase\|Histone methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Arath]]
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Du, J]]		[[Category: Du, J]]
	[[Category: Li, S]]		[[Category: Li, S]]

OCA at 14:02, 4 August 2016

OCA — Thu, 04 Aug 2016 14:02:13 GMT

←Older revision		Revision as of 14:02, 4 August 2016
Line 1:		Line 1:
		+
	==crystal structure of KRYPTONITE in complex with mCHG DNA and SAH==		==crystal structure of KRYPTONITE in complex with mCHG DNA and SAH==
	<StructureSection load='4qep' size='340' side='right' caption='[[4qep]], [[Resolution\|resolution]] 3.10Å' scene=''>		<StructureSection load='4qep' size='340' side='right' caption='[[4qep]], [[Resolution\|resolution]] 3.10Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4qen\|4qen]], [[4qeo\|4qeo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4qen\|4qen]], [[4qeo\|4qeo]]</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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [http://www.ebi.ac.uk/pdbsum/4qep 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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [http://pdbe.org/4qep PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [http://www.ebi.ac.uk/pdbsum/4qep PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qep ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4qep" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:58, 25 December 2014

OCA — Thu, 25 Dec 2014 09:58:03 GMT

←Older revision		Revision as of 09:58, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QEP FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QEP FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></td></tr>	+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4qen\|4qen]], [[4qeo\|4qeo]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4qen\|4qen]], [[4qeo\|4qeo]]</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [http://www.ebi.ac.uk/pdbsum/4qep 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=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [http://www.ebi.ac.uk/pdbsum/4qep PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/SUVH4_ARATH SUVH4_ARATH]] Histone methyltransferase. Methylates 'Lys-9' of histone H3. H3 'Lys-9' methylation represents a specific tag for epigenetic transcriptional repression. The silencing mechanism via DNA CpNpG methylation requires the targeting of chromomethylase CMT3 to methylated histones, probably through an interaction with an HP1-like adapter. By its function, KYP is directly required for the maintenance of the DNA CpNpG and asymmetric methylation. Involved in the silencing of transposable elements.<ref>PMID:11898023</ref> <ref>PMID:15457214</ref> <ref>PMID:15598823</ref> <ref>PMID:16277745</ref> <ref>PMID:16287862</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 24:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
-	[[Category: Du, J.]]	+	[[Category: Du, J]]
-	[[Category: Li, S.]]	+	[[Category: Li, S]]
-	[[Category: Patel, D J.]]	+	[[Category: Patel, D J]]
	[[Category: Histone methylation]]		[[Category: Histone methylation]]
	[[Category: Methylated dna]]		[[Category: Methylated dna]]

OCA at 07:36, 30 July 2014

OCA — Wed, 30 Jul 2014 07:36:55 GMT

←Older revision		Revision as of 07:36, 30 July 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==crystal structure of KRYPTONITE in complex with mCHG DNA and SAH==
		+	<StructureSection load='4qep' size='340' side='right' caption='[[4qep]], [[Resolution\|resolution]] 3.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4qep]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QEP FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=5CM:5-METHYL-2-DEOXY-CYTIDINE-5-MONOPHOSPHATE'>5CM</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4qen\|4qen]], [[4qeo\|4qeo]]</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qep RCSB], [http://www.ebi.ac.uk/pdbsum/4qep PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	In Arabidopsis, CHG DNA methylation is controlled by the H3K9 methylation mark through a self-reinforcing loop between DNA methyltransferase CHROMOMETHYLASE3 (CMT3) and H3K9 histone methyltransferase KRYPTONITE/SUVH4 (KYP). We report on the structure of KYP in complex with methylated DNA, substrate H3 peptide, and cofactor SAH, thereby defining the spatial positioning of the SRA domain relative to the SET domain. The methylated DNA is bound by the SRA domain with the 5mC flipped out of the DNA, while the H3(1-15) peptide substrate binds between the SET and post-SET domains, with the epsilon-ammonium of K9 positioned adjacent to bound SAH. These structural insights, complemented by functional data on key mutants of residues lining the 5mC and H3K9-binding pockets within KYP, establish how methylated DNA recruits KYP to the histone substrate. Together, the structures of KYP and previously reported CMT3 complexes provide insights into molecular mechanisms linking DNA and histone methylation.

-	~~The entry 4qep is ON HOLD until Paper Publication~~	+	Mechanism of DNA Methylation-Directed Histone Methylation by KRYPTONITE.,Du J, Johnson LM, Groth M, Feng S, Hale CJ, Li S, Vashisht AA, Gallego-Bartolome J, Wohlschlegel JA, Patel DJ, Jacobsen SE Mol Cell. 2014 Jul 9. pii: S1097-2765(14)00491-2. doi:, 10.1016/j.molcel.2014.06.009. PMID:25018018<ref>PMID:25018018</ref>

-	~~Authors~~: Du, J., Li, S., Patel, D.J.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~crystal structure of KRYPTONITE in~~ complex ~~with mCHG DNA and SAH~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Du, J.]]
		+	[[Category: Li, S.]]
		+	[[Category: Patel, D J.]]
		+	[[Category: Histone methylation]]
		+	[[Category: Methylated dna]]
		+	[[Category: Methylation]]
		+	[[Category: Set]]
		+	[[Category: Sra]]
		+	[[Category: Transcription-dna complex]]

OCA at 08:04, 11 June 2014

OCA — Wed, 11 Jun 2014 08:04:09 GMT

←Older revision		Revision as of 08:04, 11 June 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4qep is ON HOLD	+	The entry 4qep is ON HOLD until Paper Publication

	Authors: Du, J., Li, S., Patel, D.J.		Authors: Du, J., Li, S., Patel, D.J.

	Description: crystal structure of KRYPTONITE in complex with mCHG DNA and SAH		Description: crystal structure of KRYPTONITE in complex with mCHG DNA and SAH

OCA: Protected "4qep" [edit=sysop:move=sysop]

OCA — Wed, 28 May 2014 08:31:28 GMT

Protected "4qep" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:31, 28 May 2014

OCA: New page: '''Unreleased structure''' The entry 4qep is ON HOLD Authors: Du, J., Li, S., Patel, D.J. Description: crystal structure of KRYPTONITE in complex with mCHG DNA and SAH

OCA — Wed, 28 May 2014 08:31:26 GMT

New page: '''Unreleased structure''' The entry 4qep is ON HOLD Authors: Du, J., Li, S., Patel, D.J. Description: crystal structure of KRYPTONITE in complex with mCHG DNA and SAH

New page

'''Unreleased structure'''

The entry 4qep is ON HOLD

Authors: Du, J., Li, S., Patel, D.J.

Description: crystal structure of KRYPTONITE in complex with mCHG DNA and SAH