5b32: Difference between revisions

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<StructureSection load='5b32' size='340' side='right'caption='[[5b32]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='5b32' size='340' side='right'caption='[[5b32]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5b32]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B32 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5b32]] 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=5B32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B32 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b33|5b33]], [[5b31|5b31]]</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=5b32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b32 OCA], [https://pdbe.org/5b32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b32 RCSB], [https://www.ebi.ac.uk/pdbsum/5b32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b32 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=5b32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b32 OCA], [http://pdbe.org/5b32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b32 RCSB], [http://www.ebi.ac.uk/pdbsum/5b32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b32 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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> 
[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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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arimura, Y]]
[[Category: Arimura Y]]
[[Category: Horikoshi, N]]
[[Category: Horikoshi N]]
[[Category: Kurumizaka, H]]
[[Category: Kurumizaka H]]
[[Category: Taguchi, H]]
[[Category: Taguchi H]]
[[Category: Dna binding protein]]
[[Category: Histone variant]]
[[Category: Nucleosome]]
[[Category: Protein-dna complex]]

Revision as of 09:37, 31 May 2023

The crystal structure of the heterotypic H2AZ/H2A nucleosome with H3.3.The crystal structure of the heterotypic H2AZ/H2A nucleosome with H3.3.

Structural highlights

5b32 is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

H33_HUMAN

Publication Abstract from PubMed

H2A.Z is incorporated into nucleosomes located around transcription start sites and functions as an epigenetic regulator for the transcription of certain genes. During transcriptional regulation, the heterotypic H2A.Z/H2A nucleosome containing one each of H2A.Z and H2A is formed. However, previous homotypic H2A.Z nucleosome structures suggested that the L1 loop region of H2A.Z would sterically clash with the corresponding region of canonical H2A in the heterotypic nucleosome. To resolve this issue, we determined the crystal structures of heterotypic H2A.Z/H2A nucleosomes. In the H2A.Z/H2A nucleosome structure, the H2A.Z L1 loop structure was drastically altered without any structural changes of the canonical H2A L1 loop, thus avoiding the steric clash. Unexpectedly, the heterotypic H2A.Z/H2A nucleosome is more stable than the homotypic H2A.Z nucleosome. These data suggested that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome.

Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A.,Horikoshi N, Arimura Y, Taguchi H, Kurumizaka H Open Biol. 2016 Jun;6(6). pii: 160127. doi: 10.1098/rsob.160127. PMID:27358293[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Horikoshi N, Arimura Y, Taguchi H, Kurumizaka H. Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A. Open Biol. 2016 Jun;6(6). pii: 160127. doi: 10.1098/rsob.160127. PMID:27358293 doi:http://dx.doi.org/10.1098/rsob.160127

5b32, resolution 2.35Å

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