5b0y: Difference between revisions
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New page: '''Unreleased structure''' The entry 5b0y is ON HOLD Authors: Suzuki, Y., Horikoshi, N., Kurumizaka, H. Description: Category: Unreleased Structures Category: Kurumizaka, H [[... |
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The | ==Crystal structure of the nucleosome containing histone H3 with the crotonylated lysine 122== | ||
<StructureSection load='5b0y' size='340' side='right'caption='[[5b0y]], [[Resolution|resolution]] 2.56Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5b0y]] 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=5B0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B0Y FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.557Å</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=KCR:N-6-CROTONYL-L-LYSINE'>KCR</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=5b0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0y OCA], [https://pdbe.org/5b0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b0y RCSB], [https://www.ebi.ac.uk/pdbsum/5b0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0y ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/H2A1B_HUMAN H2A1B_HUMAN] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5b0y" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
*[[Histone 3D structures|Histone 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Horikoshi N]] | |||
[[Category: Kurumizaka H]] | |||
[[Category: Suzuki Y]] | |||
Latest revision as of 18:54, 8 November 2023
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
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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