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5b33

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==The crystal structure of the H2AZ nucleosome with H3.3.==
==The crystal structure of the H2AZ nucleosome with H3.3.==
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<StructureSection load='5b33' size='340' side='right' caption='[[5b33]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
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<StructureSection load='5b33' size='340' side='right'caption='[[5b33]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b33]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B33 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5b33]] is a 10 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=5B33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B33 FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b32|5b32]], [[5b31|5b31]]</td></tr>
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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]] 2.925&#8491;</td></tr>
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<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=5b33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b33 OCA], [http://pdbe.org/5b33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b33 RCSB], [http://www.ebi.ac.uk/pdbsum/5b33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b33 ProSAT]</span></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=5b33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b33 OCA], [https://pdbe.org/5b33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b33 RCSB], [https://www.ebi.ac.uk/pdbsum/5b33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b33 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_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> [[http://www.uniprot.org/uniprot/H2AZ_HUMAN H2AZ_HUMAN]] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.<ref>PMID:15878876</ref>
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[https://www.uniprot.org/uniprot/H33_HUMAN H33_HUMAN]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5b33" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5b33" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Histone 3D structures|Histone 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arimura, Y]]
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[[Category: Homo sapiens]]
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[[Category: Horikoshi, N]]
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[[Category: Large Structures]]
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[[Category: Kurumizaka, H]]
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[[Category: Arimura Y]]
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[[Category: Taguchi, H]]
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[[Category: Horikoshi N]]
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[[Category: Dna binding protein]]
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[[Category: Kurumizaka H]]
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[[Category: Histone variant]]
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[[Category: Taguchi H]]
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[[Category: Nucleosome]]
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[[Category: Protein-dna complex]]
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Current revision

The crystal structure of the H2AZ nucleosome with H3.3.

PDB ID 5b33

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