View source for 7pet


==The 4x177 nucleosome array containing H1==
<StructureSection load='7pet' size='340' side='right'caption='[[7pet]], [[Resolution|resolution]] 9.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pet]] is a 36 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PET OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PET FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9.5&#8491;</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=7pet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pet OCA], [https://pdbe.org/7pet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pet RCSB], [https://www.ebi.ac.uk/pdbsum/7pet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pet ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Throughout the genome, nucleosomes often form regular arrays that differ in nucleosome repeat length (NRL), occupancy of linker histone H1 and transcriptional activity. Here, we report cryo-EM structures of human H1-containing tetranucleosome arrays with four physiologically relevant NRLs. The structures show a zig-zag arrangement of nucleosomes, with nucleosomes 1 and 3 forming a stack. H1 binding to stacked nucleosomes depends on the NRL, whereas H1 always binds to the non-stacked nucleosomes 2 and 4. Short NRLs lead to altered trajectories of linker DNA, and these altered trajectories sterically impair H1 binding to the stacked nucleosomes in our structures. As the NRL increases, linker DNA trajectories relax, enabling H1 contacts and binding. Our results provide an explanation for why arrays with short NRLs are depleted of H1 and suited for transcription, whereas arrays with long NRLs show full H1 occupancy and can form transcriptionally silent heterochromatin regions.

Histone H1 binding to nucleosome arrays depends on linker DNA length and trajectory.,Dombrowski M, Engeholm M, Dienemann C, Dodonova S, Cramer P Nat Struct Mol Biol. 2022 May;29(5):493-501. doi: 10.1038/s41594-022-00768-w. , Epub 2022 May 17. PMID:35581345<ref>PMID:35581345</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pet" style="background-color:#fffaf0;"></div>

==See Also==
*[[Histone 3D structures|Histone 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Cramer P]]
[[Category: Dombrowski M]]