4ld9 - Revision history

OCA at 10:53, 14 December 2022

OCA — Wed, 14 Dec 2022 10:53:14 GMT

←Older revision		Revision as of 10:53, 14 December 2022
Line 1:		Line 1:

	==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle==		==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle==
-	<StructureSection load='4ld9' size='340' side='right' caption='[[4ld9]], [[Resolution\|resolution]] 3.31Å' scene=''>	+	<StructureSection load='4ld9' size='340' side='right'caption='[[4ld9]], [[Resolution\|resolution]] 3.31Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ld9]] 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=4LD9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LD9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ld9]] 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=4LD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LD9 FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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'>[https://proteopedia.org/fgij/fg.htm?mol=4ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld9 OCA], [https://pdbe.org/4ld9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ld9 RCSB], [https://www.ebi.ac.uk/pdbsum/4ld9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld9 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=4ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld9 OCA], [~~http~~://pdbe.org/4ld9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ld9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ld9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld9 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/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 21:		Line 20:

	==See Also==		==See Also==
-	*[[Histone\|Histone]]	+	*[[Histone 3D structures\|Histone 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~African clawed frog~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Baker's yeast~~]]	+	[[Category: Saccharomyces cerevisiae S288C]]
-	[[Category: Arnaudo, N]]	+	[[Category: Xenopus laevis]]
-	[[Category: Fernandez~~, I S~~]]	+	[[Category: Arnaudo N]]
-	[[Category: Martino, F]]	+	[[Category: Fernandez IS]]
-	[[Category: McLaughlin~~, S H~~]]	+	[[Category: Martino F]]
-	[[Category: Peak-Chew~~, S Y~~]]	+	[[Category: McLaughlin SH]]
-	[[Category: Rhodes, D]]	+	[[Category: Peak-Chew SY]]
-	~~[[Category: Alpha-helix]]~~	+	[[Category: Rhodes D]]
-	~~[[Category: Beta barrel]]~~	+
-	~~[[Category: Beta-sheet]]~~	+
-	~~[[Category: Chromatin]]~~	+
-	~~[[Category: Chromatin binding]]~~	+
-	~~[[Category: Double helix]]~~	+
-	~~[[Category: Double stranded dna]]~~	+
-	~~[[Category: N-terminal acetylation]]~~	+
-	~~[[Category: Nuclear protein-transcription-dna complex]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Protein-dna complex~~]]	+

OCA at 22:48, 4 August 2016

OCA — Thu, 04 Aug 2016 22:48:30 GMT

←Older revision		Revision as of 22:48, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle==		==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle==
	<StructureSection load='4ld9' size='340' side='right' caption='[[4ld9]], [[Resolution\|resolution]] 3.31Å' scene=''>		<StructureSection load='4ld9' size='340' side='right' caption='[[4ld9]], [[Resolution\|resolution]] 3.31Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ld9]] 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=4LD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LD9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ld9]] 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=4LD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LD9 FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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=4ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ld9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ld9 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=4ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld9 OCA], [http://pdbe.org/4ld9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ld9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ld9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ld9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4ld9" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 24:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Saccharomyces cerevisiae s288c~~]]	+	[[Category: African clawed frog]]
-	[[Category: ~~Xenopus laevis~~]]	+	[[Category: Baker's yeast]]
	[[Category: Arnaudo, N]]		[[Category: Arnaudo, N]]
	[[Category: Fernandez, I S]]		[[Category: Fernandez, I S]]

OCA at 13:44, 25 December 2014

OCA — Thu, 25 Dec 2014 13:44:48 GMT

←Older revision		Revision as of 13:44, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4ld9\| PDB=4ld9 \| SCENE= }}~~	+	==Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle==
-	===Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle===	+	<StructureSection load='4ld9' size='340' side='right' caption='[[4ld9]], [[Resolution\|resolution]] 3.31Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23934150}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4ld9]] 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=4LD9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LD9 FirstGlance]. <br>
-	==Function==	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">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=4ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ld9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ld9 RCSB], [http://www.ebi.ac.uk/pdbsum/4ld9 PDBsum]</span></td></tr>
		+	</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.		[[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;">
		+	== Publication Abstract from PubMed ==
		+	The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.
		+
		+	The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.,Arnaudo N, Fernandez IS, McLaughlin SH, Peak-Chew SY, Rhodes D, Martino F Nat Struct Mol Biol. 2013 Aug 11. doi: 10.1038/nsmb.2641. PMID:23934150<ref>PMID:23934150</ref>

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4ld9]] 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=4LD9 OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:023934150</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Histone\|Histone]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
	[[Category: Xenopus laevis]]		[[Category: Xenopus laevis]]
-	[[Category: Arnaudo, N.]]	+	[[Category: Arnaudo, N]]
-	[[Category: Fernandez, I S.]]	+	[[Category: Fernandez, I S]]
-	[[Category: Martino, F.]]	+	[[Category: Martino, F]]
-	[[Category: McLaughlin, S H.]]	+	[[Category: McLaughlin, S H]]
-	[[Category: Peak-Chew, S Y.]]	+	[[Category: Peak-Chew, S Y]]
-	[[Category: Rhodes, D.]]	+	[[Category: Rhodes, D]]
	[[Category: Alpha-helix]]		[[Category: Alpha-helix]]
	[[Category: Beta barrel]]		[[Category: Beta barrel]]

OCA at 05:14, 28 August 2013

OCA — Wed, 28 Aug 2013 05:14:29 GMT

←Older revision		Revision as of 05:14, 28 August 2013
Line 1:		Line 1:
	{{STRUCTURE_4ld9\| PDB=4ld9 \| SCENE= }}		{{STRUCTURE_4ld9\| PDB=4ld9 \| SCENE= }}
	===Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle===		===Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle===
		+	{{ABSTRACT_PUBMED_23934150}}

	==Function==		==Function==
Line 7:		Line 8:
	==About this Structure==		==About this Structure==
	[[4ld9]] 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=4LD9 OCA].		[[4ld9]] 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=4LD9 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:023934150</ref><references group="xtra"/><references/>
	[[Category: Saccharomyces cerevisiae s288c]]		[[Category: Saccharomyces cerevisiae s288c]]
	[[Category: Xenopus laevis]]		[[Category: Xenopus laevis]]

OCA at 08:00, 14 August 2013

OCA — Wed, 14 Aug 2013 08:00:59 GMT

←Older revision		Revision as of 08:00, 14 August 2013
Line 1:		Line 1:
-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4ld9\| PDB=4ld9 \| SCENE= }}
		+	===Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle===

-	The ~~entry 4ld9~~ is ~~ON HOLD until Paper Publication~~	+	==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.

-	~~Authors~~: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.Y., Rhodes, D.~~, Martino, F.~~	+	==About this Structure==
-		+	[[4ld9]] 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=4LD9 OCA].
-	~~Description~~: ~~Crystal structure of the~~ N-~~terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle~~	+	[[Category: Saccharomyces cerevisiae s288c]]
		+	[[Category: Xenopus laevis]]
		+	[[Category: Arnaudo, N.]]
		+	[[Category: Fernandez, I S.]]
		+	[[Category: Martino, F.]]
		+	[[Category: McLaughlin, S H.]]
		+	[[Category: Peak-Chew, S Y.]]
		+	[[Category: Rhodes, D.]]
		+	[[Category: Alpha-helix]]
		+	[[Category: Beta barrel]]
		+	[[Category: Beta-sheet]]
		+	[[Category: Chromatin]]
		+	[[Category: Chromatin binding]]
		+	[[Category: Double helix]]
		+	[[Category: Double stranded dna]]
		+	[[Category: N-terminal acetylation]]
		+	[[Category: Nuclear protein-transcription-dna complex]]
		+	[[Category: Nucleus]]
		+	[[Category: Protein-dna complex]]

OCA at 20:07, 7 August 2013

OCA — Wed, 07 Aug 2013 20:07:35 GMT

←Older revision		Revision as of 20:07, 7 August 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ld9 is ON HOLD until ~~sometime in the future~~	+	The entry 4ld9 is ON HOLD until Paper Publication

-	Authors: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.J., Rhodes, D., Martino, F.	+	Authors: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.Y., Rhodes, D., Martino, F.

-	Description: ~~Structure~~ of ~~a chromatin factor~~	+	Description: Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle

OCA at 04:16, 1 August 2013

OCA — Thu, 01 Aug 2013 04:16:41 GMT

←Older revision		Revision as of 04:16, 1 August 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4ld9 is ON HOLD	+	The entry 4ld9 is ON HOLD until sometime in the future

	Authors: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.J., Rhodes, D., Martino, F.		Authors: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.J., Rhodes, D., Martino, F.

	Description: Structure of a chromatin factor		Description: Structure of a chromatin factor

OCA: Protected "4ld9" [edit=sysop:move=sysop]

OCA — Wed, 03 Jul 2013 13:24:59 GMT

Protected "4ld9" [edit=sysop:move=sysop]

←Older revision

Revision as of 13:24, 3 July 2013

OCA: New page: '''Unreleased structure''' The entry 4ld9 is ON HOLD Authors: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.J., Rhodes, D., Martino, F. Description: Structure of a chrom...

OCA — Wed, 03 Jul 2013 13:24:58 GMT

New page: '''Unreleased structure''' The entry 4ld9 is ON HOLD Authors: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.J., Rhodes, D., Martino, F. Description: Structure of a chrom...

New page

'''Unreleased structure'''

The entry 4ld9 is ON HOLD

Authors: Arnaudo, N., Fernandez, I.S., McLaughlin, S.H., Peak-Chew, S.J., Rhodes, D., Martino, F.

Description: Structure of a chromatin factor