8x19 - Revision history

OCA at 19:58, 29 May 2024

2024-05-29T19:58:46Z

←Older revision		Revision as of 19:58, 29 May 2024
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	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/H2A1C_HUMAN H2A1C_HUMAN] 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/H2A1C_HUMAN H2A1C_HUMAN] 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 ==
		+	Histone variant H2A.Z is found at promoters and regulates transcription. The ATP-dependent chromatin remodeler SRCAP complex (SRCAP-C) promotes the replacement of canonical histone H2A-H2B dimer with H2A.Z-H2B dimer. Here, we determined structures of human SRCAP-C bound to H2A-containing nucleosome at near-atomic resolution. The SRCAP subunit integrates a 6-subunit actin-related protein (ARP) module and an ATPase-containing motor module. The ATPase-associated ARP module encircles half of the nucleosome along the DNA and may restrain net DNA translocation, a unique feature of SRCAP-C. The motor module adopts distinct nucleosome binding modes in the apo (nucleotide-free), ADP-bound, and ADP-BeF(x)-bound states, suggesting that ATPase-driven movement destabilizes H2A-H2B by unwrapping the entry DNA and pulls H2A-H2B out of nucleosome through the ZNHIT1 subunit. Structure-guided chromatin immunoprecipitation sequencing analysis confirmed the requirement of H2A-contacting ZNHIT1 in maintaining H2A.Z occupancy on the genome. Our study provides structural insights into the mechanism of H2A-H2A.Z exchange mediated by SRCAP-C.
		+
		+	Structural insights into histone exchange by human SRCAP complex.,Yu J, Sui F, Gu F, Li W, Yu Z, Wang Q, He S, Wang L, Xu Y Cell Discov. 2024 Feb 8;10(1):15. doi: 10.1038/s41421-023-00640-1. PMID:38331872<ref>PMID:38331872</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 8x19" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 12:12, 6 March 2024

2024-03-06T12:12:16Z

←Older revision		Revision as of 12:12, 6 March 2024
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-	'''Unreleased structure'''

-	~~The entry~~ 8x19 is ~~ON HOLD until Paper Publication~~	+	==Structure of nucleosome-bound SRCAP-C in the ADP-BeFx-bound state==
-		+	<StructureSection load='8x19' size='340' side='right'caption='[[8x19]], [[Resolution\|resolution]] 3.20Å' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[8x19]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8X19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8X19 FirstGlance]. <br>
-	~~Description~~:	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.2Å</td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8x19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8x19 OCA], [https://pdbe.org/8x19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8x19 RCSB], [https://www.ebi.ac.uk/pdbsum/8x19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8x19 ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/H2A1C_HUMAN H2A1C_HUMAN] 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.
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
		+	[[Category: Li W]]
		+	[[Category: Wang L]]
		+	[[Category: Wang Q]]
		+	[[Category: Xu Y]]
		+	[[Category: Yu J]]
		+	[[Category: Yu Z]]

OCA at 10:19, 13 December 2023

2023-12-13T10:19:40Z

←Older revision		Revision as of 10:19, 13 December 2023
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8x19 is ON HOLD	+	The entry 8x19 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "8x19" [edit=sysop:move=sysop]

2023-11-15T05:55:59Z

Protected "8x19" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:55, 15 November 2023

OCA: New page: '''Unreleased structure''' The entry 8x19 is ON HOLD Authors: Description: Category: Unreleased Structures

2023-11-15T05:55:58Z

New page: '''Unreleased structure''' The entry 8x19 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8x19 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]