7dlx

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(New page: '''Unreleased structure''' The entry 7dlx is ON HOLD Authors: Description: Category: Unreleased Structures)
Current revision (16:36, 29 November 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 7dlx is ON HOLD
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==crystal structure of H2AM4>Z-H2B==
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<StructureSection load='7dlx' size='340' side='right'caption='[[7dlx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7dlx]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_RM11-1a Saccharomyces cerevisiae RM11-1a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DLX FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.395&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7dlx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dlx OCA], [https://pdbe.org/7dlx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dlx RCSB], [https://www.ebi.ac.uk/pdbsum/7dlx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dlx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/H2B1_YEAST H2B1_YEAST] 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.<ref>PMID:11973294</ref> <ref>PMID:12152067</ref> <ref>PMID:14752010</ref> <ref>PMID:15280549</ref> <ref>PMID:15652479</ref> <ref>PMID:15970663</ref> <ref>PMID:15632126</ref> <ref>PMID:15632065</ref> <ref>PMID:16598039</ref> [https://www.uniprot.org/uniprot/H2A1_YEAST H2A1_YEAST] Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.<ref>PMID:11140636</ref> <ref>PMID:15458641</ref> <ref>PMID:15610741</ref> <ref>PMID:16299494</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The multisubunit chromatin remodeler SWR1/SRCAP/p400 replaces the nucleosomal H2A-H2B dimer with the free-form H2A.Z-H2B dimer, but the mechanism governing the unidirectional H2A-to-H2A.Z exchange remains elusive. Here, we perform single-molecule force spectroscopy to dissect the disassembly/reassembly processes of the H2A nucleosome and H2A.Z nucleosome. We find that the N-terminal 1-135 residues of yeast SWR1 complex protein 2 (previously termed Swc2-Z) facilitate the disassembly of nucleosomes containing H2A but not H2A.Z. The Swc2-mediated nucleosome disassembly/reassembly requires the inherently unstable H2A nucleosome, whose instability is conferred by three H2A alpha2-helical residues, Gly47, Pro49, and Ile63, as they selectively weaken the structural rigidity of the H2A-H2B dimer. It also requires Swc2-ZN (residues 1-37) that directly anchors to the H2A nucleosome and functions in the SWR1-catalyzed H2A.Z replacement in vitro and yeast H2A.Z deposition in vivo. Our findings provide mechanistic insights into how the SWR1 complex discriminates between the H2A nucleosome and H2A.Z nucleosome, establishing a simple paradigm for the governance of unidirectional H2A.Z exchange.
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Authors:
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Recognition of the inherently unstable H2A nucleosome by Swc2 is a major determinant for unidirectional H2A.Z exchange.,Dai L, Xiao X, Pan L, Shi L, Xu N, Zhang Z, Feng X, Ma L, Dou S, Wang P, Zhu B, Li W, Zhou Z Cell Rep. 2021 May 25;35(8):109183. doi: 10.1016/j.celrep.2021.109183. PMID:34038732<ref>PMID:34038732</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 7dlx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae RM11-1a]]
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[[Category: Dai LC]]
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[[Category: Zhou Z]]

Current revision

crystal structure of H2AM4>Z-H2B

PDB ID 7dlx

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