3tu4 - Revision history

OCA at 10:12, 1 March 2024

OCA — Fri, 01 Mar 2024 10:12:50 GMT

←Older revision		Revision as of 10:12, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3tu4' size='340' side='right'caption='[[3tu4]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='3tu4' size='340' side='right'caption='[[3tu4]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tu4]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/~~African_clawed_frog African clawed frog~~] and [https://en.wikipedia.org/wiki/~~Baker's_yeast Baker's yeast~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TU4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tu4]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TU4 FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~hist1h2aj~~, ~~LOC494591 (~~[~~https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog~~]~~), SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=559292 Baker's yeast])~~</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]] 3Å</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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [https://pdbe.org/3tu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [https://www.ebi.ac.uk/pdbsum/3tu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tu4 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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [https://pdbe.org/3tu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [https://www.ebi.ac.uk/pdbsum/3tu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tu4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://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. [[https://www.uniprot.org/uniprot/SIR3_YEAST SIR3_YEAST]] The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form. [[https://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.	+	[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;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component.	+
-		+
-	Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution.,Armache KJ, Garlick JD, Canzio D, Narlikar GJ, Kingston RE Science. 2011 Nov 18;334(6058):977-82. PMID:22096199<ref>PMID:22096199</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3tu4" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Histone 3D structures\|Histone 3D structures]]		*[[Histone 3D structures\|Histone 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: African clawed frog]]
-	[[Category: Baker's yeast]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Armache, K J~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: ~~Canzio, D~~]]	+	[[Category: Xenopus laevis]]
-	[[Category: ~~Garlick,~~ J D]]	+	[[Category: Armache K-J]]
-	[[Category: ~~Kingston, R E~~]]	+	[[Category: Canzio D]]
-	[[Category: ~~Narlikar, G J~~]]	+	[[Category: Garlick JD]]
-	[[Category: ~~Gene silencing~~]]	+	[[Category: Kingston RE]]
-	[[Category: ~~Histone]]~~	+	[[Category: Narlikar GJ]]
-	~~[[Category: Nucleosome]]~~	+
-	~~[[Category: Signaling protein-structural protein-dna complex~~]]	+

OCA at 05:45, 13 July 2022

OCA — Wed, 13 Jul 2022 05:45:39 GMT

←Older revision		Revision as of 05:45, 13 July 2022
Line 1:		Line 1:

	==Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.==		==Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.==
-	<StructureSection load='3tu4' size='340' side='right' caption='[[3tu4]], [[Resolution\|resolution]] 3.00Å' scene=''>	+	<StructureSection load='3tu4' size='340' side='right'caption='[[3tu4]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tu4]] is a 12 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [~~http~~://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3TU4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tu4]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TU4 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hist1h2aj, LOC494591 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hist1h2aj, LOC494591 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [~~http~~://pdbe.org/3tu4 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3tu4 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3tu4 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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [https://pdbe.org/3tu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [https://www.ebi.ac.uk/pdbsum/3tu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tu4 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~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. [[~~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/SIR3_YEAST SIR3_YEAST]] The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form. [[~~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.	+	[[https://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. [[https://www.uniprot.org/uniprot/SIR3_YEAST SIR3_YEAST]] The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form. [[https://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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 20:

	==See Also==		==See Also==
-	*[[Histone\|Histone]]	+	*[[Histone 3D structures\|Histone 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 27:
	[[Category: African clawed frog]]		[[Category: African clawed frog]]
	[[Category: Baker's yeast]]		[[Category: Baker's yeast]]
		+	[[Category: Large Structures]]
	[[Category: Armache, K J]]		[[Category: Armache, K J]]
	[[Category: Canzio, D]]		[[Category: Canzio, D]]

OCA at 22:52, 4 August 2016

OCA — Thu, 04 Aug 2016 22:52:03 GMT

←Older revision		Revision as of 22:52, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.==		==Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.==
	<StructureSection load='3tu4' size='340' side='right' caption='[[3tu4]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='3tu4' size='340' side='right' caption='[[3tu4]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c~~] and [http://en.wikipedia.org/wiki/~~Xenopus_laevis Xenopus laevis~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TU4 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog] and [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TU4 FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hist1h2aj, LOC494591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 ~~Xenopus laevis~~]), SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 ~~Saccharomyces cerevisiae S288c~~])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hist1h2aj, LOC494591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog]), SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [http://www.ebi.ac.uk/pdbsum/3tu4 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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [http://pdbe.org/3tu4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [http://www.ebi.ac.uk/pdbsum/3tu4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tu4 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 3tu4" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 23:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Saccharomyces cerevisiae s288c~~]]	+	[[Category: African clawed frog]]
-	[[Category: ~~Xenopus laevis~~]]	+	[[Category: Baker's yeast]]
	[[Category: Armache, K J]]		[[Category: Armache, K J]]
	[[Category: Canzio, D]]		[[Category: Canzio, D]]

OCA at 13:46, 25 December 2014

OCA — Thu, 25 Dec 2014 13:46:11 GMT

←Older revision		Revision as of 13:46, 25 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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [http://www.ebi.ac.uk/pdbsum/3tu4 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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [http://www.ebi.ac.uk/pdbsum/3tu4 PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[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. [[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/SIR3_YEAST SIR3_YEAST]] The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form. [[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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 16:39, 9 December 2014

OCA — Tue, 09 Dec 2014 16:39:08 GMT

←Older revision		Revision as of 16:39, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3tu4.~~png~~\|~~left\|200px~~]]	+	==Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.==
		+	<StructureSection load='3tu4' size='340' side='right' caption='[[3tu4]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TU4 FirstGlance]. <br>
		+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">hist1h2aj, LOC494591 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 Xenopus laevis]), SIR3, CMT1, MAR2, STE8, YLR442C, L9753.10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Saccharomyces cerevisiae S288c])</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=3tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tu4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tu4 RCSB], [http://www.ebi.ac.uk/pdbsum/3tu4 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Gene silencing is essential for regulating cell fate in eukaryotes. Altered chromatin architectures contribute to maintaining the silenced state in a variety of species. The silent information regulator (Sir) proteins regulate mating type in Saccharomyces cerevisiae. One of these proteins, Sir3, interacts directly with the nucleosome to help generate silenced domains. We determined the crystal structure of a complex of the yeast Sir3 BAH (bromo-associated homology) domain and the nucleosome core particle at 3.0 angstrom resolution. We see multiple molecular interactions between the protein surfaces of the nucleosome and the BAH domain that explain numerous genetic mutations. These interactions are accompanied by structural rearrangements in both the nucleosome and the BAH domain. The structure explains how covalent modifications on H4K16 and H3K79 regulate formation of a silencing complex that contains the nucleosome as a central component.

-	~~{{STRUCTURE_3tu4\| PDB=3tu4 \| SCENE= }}~~	+	Structural basis of silencing: Sir3 BAH domain in complex with a nucleosome at 3.0 A resolution.,Armache KJ, Garlick JD, Canzio D, Narlikar GJ, Kingston RE Science. 2011 Nov 18;334(6058):977-82. PMID:22096199<ref>PMID:22096199</ref>

-	~~===Crystal structure~~ of the ~~Sir3 BAH domain in complex with a nucleosome core particle~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_22096199}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3tu4]] is a 12 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org~~/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA].	+

	==See Also==		==See Also==
	*[[Histone\|Histone]]		*[[Histone\|Histone]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:022096199<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
	[[Category: Xenopus laevis]]		[[Category: Xenopus laevis]]
-	[[Category: Armache, K J.]]	+	[[Category: Armache, K J]]
-	[[Category: Canzio, D.]]	+	[[Category: Canzio, D]]
-	[[Category: Garlick, J D.]]	+	[[Category: Garlick, J D]]
-	[[Category: Kingston, R E.]]	+	[[Category: Kingston, R E]]
-	[[Category: Narlikar, G J.]]	+	[[Category: Narlikar, G J]]
	[[Category: Gene silencing]]		[[Category: Gene silencing]]
	[[Category: Histone]]		[[Category: Histone]]
	[[Category: Nucleosome]]		[[Category: Nucleosome]]
	[[Category: Signaling protein-structural protein-dna complex]]		[[Category: Signaling protein-structural protein-dna complex]]

OCA at 17:25, 20 October 2012

OCA — Sat, 20 Oct 2012 17:25:06 GMT

←Older revision		Revision as of 17:25, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3tu4]] is a 12 chain structure ~~of [[Histone]]~~ with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA].	+	[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA].

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

OCA at 00:49, 27 July 2012

OCA — Fri, 27 Jul 2012 00:49:30 GMT

←Older revision		Revision as of 00:49, 27 July 2012
Line 1:		Line 1:
	[[Image:3tu4.png\|left\|200px]]		[[Image:3tu4.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3tu4", 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_3tu4\| PDB=3tu4 \| SCENE= }}		{{STRUCTURE_3tu4\| PDB=3tu4 \| SCENE= }}

	===Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.===		===Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_22096199}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 22096199 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_22096199}}		{{ABSTRACT_PUBMED_22096199}}

	==About this Structure==		==About this Structure==
-	[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA].	+	[[3tu4]] is a 12 chain structure of [[Histone]] with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA].
		+
		+	==See Also==
		+	*[[Histone\|Histone]]

	==Reference==		==Reference==

OCA at 07:19, 7 December 2011

OCA — Wed, 07 Dec 2011 07:19:16 GMT

←Older revision		Revision as of 07:19, 7 December 2011
Line 1:		Line 1:
-	[[Image:3tu4.~~jpg~~\|left\|200px]]	+	[[Image:3tu4.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 9:
	{{STRUCTURE_3tu4\| PDB=3tu4 \| SCENE= }}		{{STRUCTURE_3tu4\| PDB=3tu4 \| SCENE= }}

-	===Crystal structure of ~~a chromatin factor~~ in complex with ~~the~~ nucleosome core particle===	+	===Crystal structure of the Sir3 BAH domain in complex with a nucleosome core particle.===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22096199}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22096199 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22096199}}

	==About this Structure==		==About this Structure==
	[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA].		[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022096199</ref><references group="xtra"/>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
	[[Category: Xenopus laevis]]		[[Category: Xenopus laevis]]
	[[Category: Armache, K J.]]		[[Category: Armache, K J.]]
		+	[[Category: Canzio, D.]]
		+	[[Category: Garlick, J D.]]
		+	[[Category: Kingston, R E.]]
		+	[[Category: Narlikar, G J.]]
	[[Category: Gene silencing]]		[[Category: Gene silencing]]
	[[Category: Histone]]		[[Category: Histone]]
	[[Category: Nucleosome]]		[[Category: Nucleosome]]
	[[Category: Signaling protein-structural protein-dna complex]]		[[Category: Signaling protein-structural protein-dna complex]]

OCA at 19:17, 23 November 2011

OCA — Wed, 23 Nov 2011 19:17:55 GMT

←Older revision		Revision as of 19:17, 23 November 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3tu4.jpg\|left\|200px]]

-	The ~~entry 3tu4~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3tu4", 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_3tu4\| PDB=3tu4 \| SCENE= }}

-	~~Authors: Armache, K.-J.~~	+	===Crystal structure of a chromatin factor in complex with the nucleosome core particle===

-	~~Description: Crystal structure of~~ a ~~chromatin factor in complex~~ with ~~the nucleosome core particle~~	+
		+	==About this Structure==
		+	[[3tu4]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_s288c Saccharomyces cerevisiae s288c] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TU4 OCA].
		+	[[Category: Saccharomyces cerevisiae s288c]]
		+	[[Category: Xenopus laevis]]
		+	[[Category: Armache, K J.]]
		+	[[Category: Gene silencing]]
		+	[[Category: Histone]]
		+	[[Category: Nucleosome]]
		+	[[Category: Signaling protein-structural protein-dna complex]]

OCA at 11:48, 16 November 2011

OCA — Wed, 16 Nov 2011 11:48:06 GMT

←Older revision		Revision as of 11:48, 16 November 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3tu4 is ON HOLD ~~until Paper Publication~~	+	The entry 3tu4 is ON HOLD

	Authors: Armache, K.-J.		Authors: Armache, K.-J.

	Description: Crystal structure of a chromatin factor in complex with the nucleosome core particle		Description: Crystal structure of a chromatin factor in complex with the nucleosome core particle