4r8p - Revision history

OCA at 17:46, 20 September 2023

OCA — Wed, 20 Sep 2023 17:46:02 GMT

←Older revision		Revision as of 17:46, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8P FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 3.2846Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [https://pdbe.org/4r8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [https://www.ebi.ac.uk/pdbsum/4r8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8p 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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [https://pdbe.org/4r8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [https://www.ebi.ac.uk/pdbsum/4r8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8p ProSAT]</span></td></tr>
	</table>		</table>

OCA at 06:44, 2 March 2023

OCA — Thu, 02 Mar 2023 06:44:38 GMT

←Older revision		Revision as of 06:44, 2 March 2023
Line 1:		Line 1:

	==Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle==		==Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle==
-	<StructureSection load='4r8p' size='340' side='right' caption='[[4r8p]], [[Resolution\|resolution]] 3.28Å' scene=''>	+	<StructureSection load='4r8p' size='340' side='right'caption='[[4r8p]], [[Resolution\|resolution]] 3.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/ ], [~~http~~://en.wikipedia.org/wiki/~~African_clawed_frog African clawed frog~~] and [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4R8P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8P FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">histone H3.2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), histone H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), hist1h2aj, LOC494591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), histone H2B 1.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), BMI1, PCGF4, RNF51 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BAP1, DING, HIPI3, RING1B, Ring1B-UbcH5c fusion, RNF2, UBC5C, UBCH5C, UBE2D3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [https://pdbe.org/4r8p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [https://www.ebi.ac.uk/pdbsum/4r8p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8p 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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [~~http~~://pdbe.org/4r8p PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4r8p PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8p ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/BMI1_HUMAN BMI1_HUMAN]] Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2.<ref>PMID:16359901</ref> <ref>PMID:16882984</ref> <ref>PMID:16714294</ref> [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/RING2_HUMAN RING2_HUMAN]] E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity.<ref>PMID:11513855</ref> <ref>PMID:15386022</ref> <ref>PMID:16359901</ref> <ref>PMID:16714294</ref> <ref>PMID:20696397</ref> [[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.	+	[https://www.uniprot.org/uniprot/H32_XENLA H32_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 19:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4r8p" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4r8p" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone 3D structures\|Histone 3D structures]]
		+	*[[Polycomb complex proteins 3D structures\|Polycomb complex proteins 3D structures]]
		+	*[[Polycomb proteins\|Polycomb proteins]]
		+	*[[Ubiquitin protein ligase 3D structures\|Ubiquitin protein ligase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~African clawed frog~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Henrici, R C~~]]	+	[[Category: Synthetic construct]]
-	[[Category: ~~McGinty, R K~~]]	+	[[Category: Xenopus laevis]]
-	[[Category: ~~Tan, S~~]]	+	[[Category: Henrici RC]]
-	[[Category: ~~Arginine anchor~~]]	+	[[Category: McGinty RK]]
-	[[Category: ~~Histone modification enzyme]]~~	+	[[Category: Tan S]]
-	~~[[Category: Ring domain]]~~	+
-	~~[[Category: Structural protein-dna complex]]~~	+
-	~~[[Category: Ubiquitin ligase~~]]	+

OCA at 02:57, 16 November 2017

OCA — Thu, 16 Nov 2017 02:57:16 GMT

←Older revision		Revision as of 02:57, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='4r8p' size='340' side='right' caption='[[4r8p]], [[Resolution\|resolution]] 3.28Å' scene=''>		<StructureSection load='4r8p' size='340' side='right' caption='[[4r8p]], [[Resolution\|resolution]] 3.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8P FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/ ], [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8P FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">histone H3.2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), histone H4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), hist1h2aj, LOC494591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), histone H2B 1.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), BMI1, PCGF4, RNF51 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), BAP1, DING, HIPI3, RING1B, Ring1B-UbcH5c fusion, RNF2, UBC5C, UBCH5C, UBE2D3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://pdbe.org/4r8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8p 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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://pdbe.org/4r8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8p ProSAT]</span></td></tr>
	</table>		</table>
Line 18:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4r8p" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4r8p" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Histone\|Histone]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: African clawed frog]]
		+	[[Category: Human]]
	[[Category: Henrici, R C]]		[[Category: Henrici, R C]]
	[[Category: McGinty, R K]]		[[Category: McGinty, R K]]

OCA at 16:53, 4 August 2016

OCA — Thu, 04 Aug 2016 16:53:51 GMT

←Older revision		Revision as of 16:53, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle==		==Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle==
	<StructureSection load='4r8p' size='340' side='right' caption='[[4r8p]], [[Resolution\|resolution]] 3.28Å' scene=''>		<StructureSection load='4r8p' size='340' side='right' caption='[[4r8p]], [[Resolution\|resolution]] 3.28Å' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8P FirstGlance]. <br>		<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8P FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p 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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://pdbe.org/4r8p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8p ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 16:		Line 17:
	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 4r8p" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Histone\|Histone]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:15, 24 December 2014

OCA — Wed, 24 Dec 2014 17:15:48 GMT

←Older revision		Revision as of 17:15, 24 December 2014
Line 6:		Line 6:
	<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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p 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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BMI1_HUMAN BMI1_HUMAN]] Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. In the PRC1 complex, it is required to stimulate the E3 ubiquitin-protein ligase activity of RNF2/RING2.<ref>PMID:16359901</ref> <ref>PMID:16882984</ref> <ref>PMID:16714294</ref> [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/RING2_HUMAN RING2_HUMAN]] E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity.<ref>PMID:11513855</ref> <ref>PMID:15386022</ref> <ref>PMID:16359901</ref> <ref>PMID:16714294</ref> <ref>PMID:20696397</ref> [[http://www.uniprot.org/uniprot/H32_XENLA H32_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. [[http://www.uniprot.org/uniprot/H2B11_XENLA H2B11_XENLA]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:47, 12 November 2014

OCA — Wed, 12 Nov 2014 07:47:40 GMT

←Older revision		Revision as of 07:47, 12 November 2014
Line 6:		Line 6:
	<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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p 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=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p PDBsum]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The Polycomb group of epigenetic enzymes represses expression of developmentally regulated genes in many eukaryotes. This group includes the Polycomb repressive complex 1 (PRC1), which ubiquitylates nucleosomal histone H2A Lys 119 using its E3 ubiquitin ligase subunits, Ring1B and Bmi1, together with an E2 ubiquitin-conjugating enzyme, UbcH5c. However, the molecular mechanism of nucleosome substrate recognition by PRC1 or other chromatin enzymes is unclear. Here we present the crystal structure of the human Ring1B-Bmi1-UbcH5c E3-E2 complex (the PRC1 ubiquitylation module) bound to its nucleosome core particle substrate. The structure shows how a chromatin enzyme achieves substrate specificity by interacting with several nucleosome surfaces spatially distinct from the site of catalysis. Our structure further reveals an unexpected role for the ubiquitin E2 enzyme in substrate recognition, and provides insight into how the related histone H2A E3 ligase, BRCA1, interacts with and ubiquitylates the nucleosome.
		+
		+	Crystal structure of the PRC1 ubiquitylation module bound to the nucleosome.,McGinty RK, Henrici RC, Tan S Nature. 2014 Oct 30;514(7524):591-6. doi: 10.1038/nature13890. PMID:25355358<ref>PMID:25355358</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Henrici, R C.]]	+	[[Category: Henrici, R C]]
-	[[Category: McGinty, R K.]]	+	[[Category: McGinty, R K]]
-	[[Category: Tan, S.]]	+	[[Category: Tan, S]]
	[[Category: Arginine anchor]]		[[Category: Arginine anchor]]
	[[Category: Histone modification enzyme]]		[[Category: Histone modification enzyme]]

OCA at 09:01, 5 November 2014

OCA — Wed, 05 Nov 2014 09:01:07 GMT

←Older revision		Revision as of 09:01, 5 November 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle==
-		+	<StructureSection load='4r8p' size='340' side='right' caption='[[4r8p]], [[Resolution\|resolution]] 3.28Å' scene=''>
-	~~The entry~~ 4r8p is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4r8p]] is a 14 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8P FirstGlance]. <br>
-	~~Authors~~: ~~McGinty~~, R.K., Henrici, R.C., Tan, S.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r8p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8p RCSB], [http://www.ebi.ac.uk/pdbsum/4r8p PDBsum]</span></td></tr>
-	~~Description~~: ~~Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle~~	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Henrici, R C.]]
		+	[[Category: McGinty, R K.]]
		+	[[Category: Tan, S.]]
		+	[[Category: Arginine anchor]]
		+	[[Category: Histone modification enzyme]]
		+	[[Category: Ring domain]]
		+	[[Category: Structural protein-dna complex]]
		+	[[Category: Ubiquitin ligase]]

OCA at 09:37, 22 October 2014

OCA — Wed, 22 Oct 2014 09:37:59 GMT

←Older revision		Revision as of 09:37, 22 October 2014
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4r8p is ON HOLD	+	The entry 4r8p is ON HOLD until Paper Publication

	Authors: McGinty, R.K., Henrici, R.C., Tan, S.		Authors: McGinty, R.K., Henrici, R.C., Tan, S.

	Description: Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle		Description: Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle

OCA: Protected "4r8p" [edit=sysop:move=sysop]

OCA — Wed, 10 Sep 2014 08:26:27 GMT

Protected "4r8p" [edit=sysop:move=sysop]

←Older revision

Revision as of 08:26, 10 September 2014

OCA: New page: '''Unreleased structure''' The entry 4r8p is ON HOLD Authors: McGinty, R.K., Henrici, R.C., Tan, S. Description: Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module ...

OCA — Wed, 10 Sep 2014 08:26:25 GMT

New page: '''Unreleased structure''' The entry 4r8p is ON HOLD Authors: McGinty, R.K., Henrici, R.C., Tan, S. Description: Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module ...

New page

'''Unreleased structure'''

The entry 4r8p is ON HOLD

Authors: McGinty, R.K., Henrici, R.C., Tan, S.

Description: Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle