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<StructureSection load='6kbb' size='340' side='right'caption='[[6kbb]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
<StructureSection load='6kbb' size='340' side='right'caption='[[6kbb]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6kbb]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KBB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KBB FirstGlance]. <br>
<table><tr><td colspan='2'>[[6kbb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KBB FirstGlance]. <br>
</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=6kbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kbb OCA], [http://pdbe.org/6kbb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kbb RCSB], [http://www.ebi.ac.uk/pdbsum/6kbb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kbb ProSAT]</span></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]] 2.365&#8491;</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=6kbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kbb OCA], [https://pdbe.org/6kbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kbb RCSB], [https://www.ebi.ac.uk/pdbsum/6kbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kbb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/H2A1D_HUMAN H2A1D_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. [[http://www.uniprot.org/uniprot/SWC5_YEAST SWC5_YEAST]] Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Involved in chromosome stability.<ref>PMID:14645854</ref> <ref>PMID:14690608</ref> <ref>PMID:15045029</ref>  [[http://www.uniprot.org/uniprot/H2B2E_HUMAN H2B2E_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.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref>   Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref>
[https://www.uniprot.org/uniprot/H2A1D_HUMAN H2A1D_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 ==
The SWR complex edits the histone composition of nucleosomes at promoters to facilitate transcription by replacing the two nucleosomal H2A-H2B (A-B) dimers with H2A.Z-H2B (Z-B) dimers. Swc5, a subunit of SWR, binds to A-B dimers, but its role in the histone replacement reaction was unclear. In this study, we showed that Swc5 uses a tandem DEF/Y motif within an intrinsically disordered region to engage the A-B dimer. A 2.37-A X-ray crystal structure of the histone binding domain of Swc5 in complex with an A-B dimer showed that consecutive acidic residues and flanking hydrophobic residues of Swc5 form a cap over the histones, excluding histone-DNA interaction. Mutations in Swc5 DEF/Y inhibited the nucleosome editing function of SWR in vitro. Swc5 DEF/Y interacts with histones in vivo, and the extent of this interaction is dependent on the remodeling ATPase of SWR, supporting a model in which Swc5 acts as a wedge to promote A-B dimer eviction. Given that DEF/Y motifs are found in other evolutionary unrelated chromatin regulators, this work provides the molecular basis for a general strategy used repeatedly during eukaryotic evolution to mobilize histones in various genomic functions.
 
Role of a DEF/Y motif in histone H2A-H2B recognition and nucleosome editing.,Huang Y, Sun L, Pierrakeas L, Dai L, Pan L, Luk E, Zhou Z Proc Natl Acad Sci U S A. 2020 Jan 30. pii: 1914313117. doi:, 10.1073/pnas.1914313117. PMID:32001508<ref>PMID:32001508</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kbb" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Histone 3D structures|Histone 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Huang, Y]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Zhou, Z]]
[[Category: Huang Y]]
[[Category: Histone chaperone]]
[[Category: Zhou Z]]
[[Category: Transcription]]

Latest revision as of 10:29, 22 November 2023

Role of the DEF/Y motif of Swc5 in histone H2A.Z deposition

6kbb, resolution 2.37Å

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