View source for 4qlc


==Crystal structure of chromatosome at 3.5 angstrom resolution==
<StructureSection load='4qlc' size='340' side='right'caption='[[4qlc]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4qlc]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster], [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QLC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QLC 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]] 3.503&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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=4qlc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qlc OCA], [https://pdbe.org/4qlc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qlc RCSB], [https://www.ebi.ac.uk/pdbsum/4qlc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qlc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H3_DROME H3_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Linker histones bind to the nucleosome and regulate the structure of chromatin and gene expression. Despite more than three decades of effort, the structural basis of nucleosome recognition by linker histones remains elusive. Here, we report the crystal structure of the globular domain of chicken linker histone H5 in complex with the nucleosome at 3.5 A resolution, which is validated using nuclear magnetic resonance spectroscopy. The globular domain sits on the dyad of the nucleosome and interacts with both DNA linkers. Our structure integrates results from mutation analyses and previous cross-linking and fluorescence recovery after photobleach experiments, and it helps resolve the long debate on structural mechanisms of nucleosome recognition by linker histones. The on-dyad binding mode of the H5 globular domain is different from the recently reported off-dyad binding mode of Drosophila linker histone H1. We demonstrate that linker histones with different binding modes could fold chromatin to form distinct higher-order structures.

Structural Mechanisms of Nucleosome Recognition by Linker Histones.,Zhou BR, Jiang J, Feng H, Ghirlando R, Xiao TS, Bai Y Mol Cell. 2015 Jul 22. pii: S1097-2765(15)00497-9. doi:, 10.1016/j.molcel.2015.06.025. PMID:26212454<ref>PMID:26212454</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4qlc" style="background-color:#fffaf0;"></div>

==See Also==
*[[Histone 3D structures|Histone 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Gallus gallus]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bai YW]]
[[Category: Jiang JS]]
[[Category: Xiao TS]]
[[Category: Zhou BR]]