5b0z: Difference between revisions
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==The crystal structure of the nucleosome containing H3.2, at 1.98 A resolution== | ==The crystal structure of the nucleosome containing H3.2, at 1.98 A resolution== | ||
<StructureSection load='5b0z' size='340' side='right' caption='[[5b0z]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='5b0z' size='340' side='right'caption='[[5b0z]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5b0z]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B0Z OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5b0z]] 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=5B0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B0Z FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.987Å</td></tr> | ||
<tr id=' | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b0z OCA], [https://pdbe.org/5b0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b0z RCSB], [https://www.ebi.ac.uk/pdbsum/5b0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b0z ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 18: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5b0z" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5b0z" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Histone 3D structures|Histone 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Horikoshi N]] | ||
[[Category: | [[Category: Kato D]] | ||
[[Category: | [[Category: Kurumizaka H]] | ||
[[Category: | [[Category: Suzuki Y]] | ||
Latest revision as of 18:54, 8 November 2023
The crystal structure of the nucleosome containing H3.2, at 1.98 A resolutionThe crystal structure of the nucleosome containing H3.2, at 1.98 A resolution
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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