5b0y: Difference between revisions

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'''Unreleased structure'''
==Crystal structure of the nucleosome containing histone H3 with the crotonylated lysine 122==
<StructureSection load='5b0y' size='340' side='right' caption='[[5b0y]], [[Resolution|resolution]] 2.56&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5b0y]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B0Y 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>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCR:N-6-CROTONYL-L-LYSINE'>KCR</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b0z|5b0z]]</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=5b0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0y OCA], [http://pdbe.org/5b0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b0y RCSB], [http://www.ebi.ac.uk/pdbsum/5b0y PDBsum]</span></td></tr>
</table>
== 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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crotonylation of histones is an important post-translational modification, and epigenetically functions in the regulation of genomic DNA activity. The histone modifications in the structured "histone-fold" domains are considered to have an especially important impact on the nucleosome structure and dynamics. In the present study, we reconstituted the human nucleosome containing histone H3.2 crotonylated at the Lys122 residue, and determined its crystal structure at 2.56 A resolution. We found that the crotonylation of the H3 Lys122 residue does not affect the overall nucleosome structure, but locally impedes the formation of the water-mediated hydrogen bond with the DNA backbone. Consistently, thermal stability assays revealed that the H3 Lys122 crotonylation, as well as the H3 Lys122 acetylation, clearly reduced the histone-DNA association.


The entry 5b0y is ON HOLD  until Paper Publication
Crystal structure of the nucleosome containing histone H3 with crotonylated lysine 122.,Suzuki Y, Horikoshi N, Kato D, Kurumizaka H Biochem Biophys Res Commun. 2016 Jan 15;469(3):483-9. doi:, 10.1016/j.bbrc.2015.12.041. Epub 2015 Dec 13. PMID:26694698<ref>PMID:26694698</ref>


Authors: Suzuki, Y., Horikoshi, N., Kurumizaka, H.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description:  
<div class="pdbe-citations 5b0y" style="background-color:#fffaf0;"></div>
[[Category: Unreleased Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Horikoshi, N]]
[[Category: Kurumizaka, H]]
[[Category: Kurumizaka, H]]
[[Category: Suzuki, Y]]
[[Category: Suzuki, Y]]
[[Category: Horikoshi, N]]
[[Category: Dna binding protein]]
[[Category: Histone modification]]
[[Category: Nucleosome]]

Revision as of 05:08, 28 January 2016

Crystal structure of the nucleosome containing histone H3 with the crotonylated lysine 122Crystal structure of the nucleosome containing histone H3 with the crotonylated lysine 122

Structural highlights

5b0y is a 10 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
NonStd Res:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.[1] [2] [3] 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.[4] [5] [6]

Publication Abstract from PubMed

The crotonylation of histones is an important post-translational modification, and epigenetically functions in the regulation of genomic DNA activity. The histone modifications in the structured "histone-fold" domains are considered to have an especially important impact on the nucleosome structure and dynamics. In the present study, we reconstituted the human nucleosome containing histone H3.2 crotonylated at the Lys122 residue, and determined its crystal structure at 2.56 A resolution. We found that the crotonylation of the H3 Lys122 residue does not affect the overall nucleosome structure, but locally impedes the formation of the water-mediated hydrogen bond with the DNA backbone. Consistently, thermal stability assays revealed that the H3 Lys122 crotonylation, as well as the H3 Lys122 acetylation, clearly reduced the histone-DNA association.

Crystal structure of the nucleosome containing histone H3 with crotonylated lysine 122.,Suzuki Y, Horikoshi N, Kato D, Kurumizaka H Biochem Biophys Res Commun. 2016 Jan 15;469(3):483-9. doi:, 10.1016/j.bbrc.2015.12.041. Epub 2015 Dec 13. PMID:26694698[7]

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

References

  1. ↑ Kim HS, Cho JH, Park HW, Yoon H, Kim MS, Kim SC. Endotoxin-neutralizing antimicrobial proteins of the human placenta. J Immunol. 2002 Mar 1;168(5):2356-64. PMID:11859126
  2. ↑ Tollin M, Bergman P, Svenberg T, Jornvall H, Gudmundsson GH, Agerberth B. Antimicrobial peptides in the first line defence of human colon mucosa. Peptides. 2003 Apr;24(4):523-30. PMID:12860195
  3. ↑ Howell SJ, Wilk D, Yadav SP, Bevins CL. Antimicrobial polypeptides of the human colonic epithelium. Peptides. 2003 Nov;24(11):1763-70. PMID:15019208 doi:10.1016/j.peptides.2003.07.028
  4. ↑ Kim HS, Cho JH, Park HW, Yoon H, Kim MS, Kim SC. Endotoxin-neutralizing antimicrobial proteins of the human placenta. J Immunol. 2002 Mar 1;168(5):2356-64. PMID:11859126
  5. ↑ Tollin M, Bergman P, Svenberg T, Jornvall H, Gudmundsson GH, Agerberth B. Antimicrobial peptides in the first line defence of human colon mucosa. Peptides. 2003 Apr;24(4):523-30. PMID:12860195
  6. ↑ Howell SJ, Wilk D, Yadav SP, Bevins CL. Antimicrobial polypeptides of the human colonic epithelium. Peptides. 2003 Nov;24(11):1763-70. PMID:15019208 doi:10.1016/j.peptides.2003.07.028
  7. ↑ Suzuki Y, Horikoshi N, Kato D, Kurumizaka H. Crystal structure of the nucleosome containing histone H3 with crotonylated lysine 122. Biochem Biophys Res Commun. 2016 Jan 15;469(3):483-9. doi:, 10.1016/j.bbrc.2015.12.041. Epub 2015 Dec 13. PMID:26694698 doi:http://dx.doi.org/10.1016/j.bbrc.2015.12.041

5b0y, resolution 2.56Å

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