4au7 - Revision history

OCA at 11:35, 20 December 2023

2023-12-20T11:35:33Z

←Older revision		Revision as of 11:35, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='4au7' size='340' side='right'caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>		<StructureSection load='4au7' size='340' side='right'caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4au7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Lk3_transgenic_mice Lk3 transgenic mice~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AU7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4au7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AU7 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=EDO:1~~,2~~-ETHANEDIOL'>EDO</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]] 2.07Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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;~~'>~~[[1f66\|1f66]], [[1u35\|1u35]], [[2wp2\|2wp2]]~~</~~div~~><~~/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=4au7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au7 OCA], [https://pdbe.org/4au7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4au7 RCSB], [https://www.ebi.ac.uk/pdbsum/4au7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4au7 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=4au7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au7 OCA], [https://pdbe.org/4au7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4au7 RCSB], [https://www.ebi.ac.uk/pdbsum/4au7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4au7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/~~SV422_MOUSE SV422_MOUSE]~~] Histone methyltransferase that specifically ~~trimethylates~~ 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. ~~SUV420H1~~ is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2).<ref>PMID:15145825</ref>	+	[https://www.uniprot.org/uniprot/KMT5C_MOUSE KMT5C_MOUSE] Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity (PubMed:15145825, PubMed:28114273). In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (By similarity). H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression (PubMed:15145825). Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions (PubMed:15145825). KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (PubMed:15750587, PubMed:16612004). Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity). May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (PubMed:28114273).[UniProtKB:Q86Y97]<ref>PMID:15145825</ref> <ref>PMID:15750587</ref> <ref>PMID:16612004</ref> <ref>PMID:28114273</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Lk3 transgenic mice~~]]	+	[[Category: Mus musculus]]
-	[[Category: Cronin~~, N B~~]]	+	[[Category: Cronin NB]]
-	[[Category: Southall~~, S M~~]]	+	[[Category: Southall SM]]
-	[[Category: Wilson~~, J R]]~~	+	[[Category: Wilson JR]]
-	~~[[Category: Epigenetic]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 05:46, 25 August 2022

2022-08-25T05:46:25Z

←Older revision		Revision as of 05:46, 25 August 2022
Line 3:		Line 3:
	<StructureSection load='4au7' size='340' side='right'caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>		<StructureSection load='4au7' size='340' side='right'caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4au7]] is a 3 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4AU7 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4au7]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AU7 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=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=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f66\|1f66]], [[1u35\|1u35]], [[2wp2\|2wp2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f66\|1f66]], [[1u35\|1u35]], [[2wp2\|2wp2]]</div></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=4au7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au7 OCA], [~~http~~://pdbe.org/4au7 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4au7 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4au7 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4au7 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=4au7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au7 OCA], [https://pdbe.org/4au7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4au7 RCSB], [https://www.ebi.ac.uk/pdbsum/4au7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4au7 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/SV422_MOUSE SV422_MOUSE]] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2).<ref>PMID:15145825</ref>	+	[[https://www.uniprot.org/uniprot/SV422_MOUSE SV422_MOUSE]] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2).<ref>PMID:15145825</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Histone methyltransferase\|Histone methyltransferase]]	+	*[[Histone methyltransferase 3D structures\|Histone methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 29:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
	[[Category: Cronin, N B]]		[[Category: Cronin, N B]]

OCA at 08:48, 6 March 2019

2019-03-06T08:48:17Z

←Older revision		Revision as of 08:48, 6 March 2019
Line 1:		Line 1:

	==The structure of the Suv4-20h2 ternary complex with histone H4==		==The structure of the Suv4-20h2 ternary complex with histone H4==
-	<StructureSection load='4au7' size='340' side='right' caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>	+	<StructureSection load='4au7' size='340' side='right'caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4au7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AU7 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4au7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AU7 FirstGlance]. <br>

OCA at 07:23, 4 August 2016

2016-08-04T07:23:27Z

←Older revision		Revision as of 07:23, 4 August 2016
Line 1:		Line 1:
		+
	==The structure of the Suv4-20h2 ternary complex with histone H4==		==The structure of the Suv4-20h2 ternary complex with histone H4==
	<StructureSection load='4au7' size='340' side='right' caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>		<StructureSection load='4au7' size='340' side='right' caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f66\|1f66]], [[1u35\|1u35]], [[2wp2\|2wp2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f66\|1f66]], [[1u35\|1u35]], [[2wp2\|2wp2]]</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=4au7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4au7 RCSB], [http://www.ebi.ac.uk/pdbsum/4au7 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=4au7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au7 OCA], [http://pdbe.org/4au7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4au7 RCSB], [http://www.ebi.ac.uk/pdbsum/4au7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4au7 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 4au7" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 06:49, 24 December 2014

2014-12-24T06:49:11Z

←Older revision		Revision as of 06:49, 24 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4au7\| PDB=4au7 \| SCENE= }}~~	+	==The structure of the Suv4-20h2 ternary complex with histone H4==
-	===The structure of the Suv4-20h2 ternary complex with histone H4===	+	<StructureSection load='4au7' size='340' side='right' caption='[[4au7]], [[Resolution\|resolution]] 2.07Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24049080}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4au7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AU7 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1f66\|1f66]], [[1u35\|1u35]], [[2wp2\|2wp2]]</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=4au7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4au7 RCSB], [http://www.ebi.ac.uk/pdbsum/4au7 PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/SV422_MOUSE SV422_MOUSE]] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2).<ref>PMID:15145825</ref>		[[http://www.uniprot.org/uniprot/SV422_MOUSE SV422_MOUSE]] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2).<ref>PMID:15145825</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The delivery of site-specific post-translational modifications to histones generates an epigenetic regulatory network that directs fundamental DNA-mediated processes and governs key stages in development. Methylation of histone H4 lysine-20 has been implicated in DNA repair, transcriptional silencing, genomic stability and regulation of replication. We present the structure of the histone H4K20 methyltransferase Suv4-20h2 in complex with its histone H4 peptide substrate and S-adenosyl methionine cofactor. Analysis of the structure reveals that the Suv4-20h2 active site diverges from the canonical SET domain configuration and generates a high degree of both substrate and product specificity. Together with supporting biochemical data comparing Suv4-20h1 and Suv4-20h2, we demonstrate that the Suv4-20 family enzymes take a previously mono-methylated H4K20 substrate and generate an exclusively di-methylated product. We therefore predict that other enzymes are responsible for the tri-methylation of histone H4K20 that marks silenced heterochromatin.

-	~~==About this Structure==~~	+	A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases.,Southall SM, Cronin NB, Wilson JR Nucleic Acids Res. 2013 Sep 18. PMID:24049080<ref>PMID:24049080</ref>
-	~~[[4au7]] is a 3 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=4AU7 OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Histone methyltransferase\|Histone methyltransferase]]		*[[Histone methyltransferase\|Histone methyltransferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:024049080</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
	[[Category: Lk3 transgenic mice]]		[[Category: Lk3 transgenic mice]]
-	[[Category: Cronin, N B.]]	+	[[Category: Cronin, N B]]
-	[[Category: Southall, S M.]]	+	[[Category: Southall, S M]]
-	[[Category: Wilson, J R.]]	+	[[Category: Wilson, J R]]
	[[Category: Epigenetic]]		[[Category: Epigenetic]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 06:51, 15 January 2014

2014-01-15T06:51:02Z

←Older revision		Revision as of 06:51, 15 January 2014
Line 1:		Line 1:
	{{STRUCTURE_4au7\| PDB=4au7 \| SCENE= }}		{{STRUCTURE_4au7\| PDB=4au7 \| SCENE= }}
	===The structure of the Suv4-20h2 ternary complex with histone H4===		===The structure of the Suv4-20h2 ternary complex with histone H4===
		+	{{ABSTRACT_PUBMED_24049080}}
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/SV422_MOUSE SV422_MOUSE]] Histone methyltransferase that specifically trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. SUV420H1 is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2).<ref>PMID:15145825</ref>

	==About this Structure==		==About this Structure==
-	[[4au7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Mus_musculus Mus musculus~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA].	+	[[4au7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA].
		+
		+	==See Also==
		+	*[[Histone methyltransferase\|Histone methyltransferase]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:024049080</ref><references group="xtra"/><references/>
	[[Category: Histone-lysine N-methyltransferase]]		[[Category: Histone-lysine N-methyltransferase]]
-	[[Category: ~~Mus musculus~~]]	+	[[Category: Lk3 transgenic mice]]
	[[Category: Cronin, N B.]]		[[Category: Cronin, N B.]]
	[[Category: Southall, S M.]]		[[Category: Southall, S M.]]

OCA at 06:24, 20 June 2013

2013-06-20T06:24:14Z

←Older revision		Revision as of 06:24, 20 June 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4au7\| PDB=4au7 \| SCENE= }}
		+	===The structure of the Suv4-20h2 ternary complex with histone H4===

-	~~The entry~~ 4au7 is ~~ON HOLD~~	+	==About this Structure==
-		+	[[4au7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU7 OCA].
-	~~Authors~~: ~~Southall, S~~.M., Cronin, N.B., Wilson, J.R.	+	[[Category: Histone-lysine N-methyltransferase]]
-		+	[[Category: Mus musculus]]
-	~~Description~~: ~~The structure of the Suv4-20h2 ternary complex with histone H4~~	+	[[Category: Cronin, N B.]]
		+	[[Category: Southall, S M.]]
		+	[[Category: Wilson, J R.]]
		+	[[Category: Epigenetic]]
		+	[[Category: Transferase]]

OCA: Protected "4au7" [edit=sysop:move=sysop]

2012-05-23T05:32:52Z

Protected "4au7" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:32, 23 May 2012

OCA: New page: '''Unreleased structure''' The entry 4au7 is ON HOLD Authors: Southall, S.M., Cronin, N.B., Wilson, J.R. Description: The structure of the Suv4-20h2 ternary complex with histone H4

2012-05-23T05:32:51Z

New page: '''Unreleased structure''' The entry 4au7 is ON HOLD Authors: Southall, S.M., Cronin, N.B., Wilson, J.R. Description: The structure of the Suv4-20h2 ternary complex with histone H4

New page

'''Unreleased structure'''

The entry 4au7 is ON HOLD

Authors: Southall, S.M., Cronin, N.B., Wilson, J.R.

Description: The structure of the Suv4-20h2 ternary complex with histone H4