8aag: Difference between revisions
New page: '''Unreleased structure''' The entry 8aag is ON HOLD Authors: Description: Category: Unreleased Structures |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==H1-bound palindromic nucleosome, state 1== | |||
<StructureSection load='8aag' size='340' side='right'caption='[[8aag]], [[Resolution|resolution]] 10.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8aag]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] 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=8AAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AAG 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]] 10Å</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=8aag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aag OCA], [https://pdbe.org/8aag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aag RCSB], [https://www.ebi.ac.uk/pdbsum/8aag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aag ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/H4_HUMAN H4_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Nucleosomes are symmetric structures. However, binding of linker histones generates an inherently asymmetric H1-nucleosome complex, and whether this asymmetry is transmitted to the overall nucleosome structure, and therefore also to chromatin, is unclear. Efforts to investigate potential asymmetry due to H1s have been hampered by the DNA sequence, which naturally differs in each gyre. To overcome this issue, we designed and analyzed by cryo-EM a nucleosome reconstituted with a palindromic (601L) 197-bp DNA. As in the non-palindromic 601 sequence, H1 restricts linker DNA flexibility but reveals partial asymmetrical unwrapping. However, in contrast to the non-palindromic nucleosome, in the palindromic nucleosome H1 CTD collapses to the proximal linker. Molecular dynamics simulations show that this could be dictated by a slightly tilted orientation of the globular domain (GD) of H1, which could be linked to the DNA sequence of the nucleosome dyad. | |||
Nucleosome dyad determines the H1 C-terminus collapse on distinct DNA arms.,Louro JA, Boopathi R, Beinsteiner B, Mohideen Patel AK, Cheng TC, Angelov D, Hamiche A, Bendar J, Kale S, Klaholz BP, Dimitrov S Structure. 2023 Feb 2;31(2):201-212.e5. doi: 10.1016/j.str.2022.12.005. Epub 2023 , Jan 6. PMID:36610392<ref>PMID:36610392</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8aag" 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: Xenopus laevis]] | |||
[[Category: Alegrio Louro J]] | |||
[[Category: Angelov D]] | |||
[[Category: Bednar J]] | |||
[[Category: Beinsteiner B]] | |||
[[Category: Boopathi R]] | |||
[[Category: Cheng TC]] | |||
[[Category: Dimitrov S]] | |||
[[Category: Hamiche A]] | |||
[[Category: Kale S]] | |||
[[Category: Klaholz B]] | |||
[[Category: Patel AKM]] | |||
Latest revision as of 09:44, 24 July 2024
H1-bound palindromic nucleosome, state 1H1-bound palindromic nucleosome, state 1
Structural highlights
FunctionPublication Abstract from PubMedNucleosomes are symmetric structures. However, binding of linker histones generates an inherently asymmetric H1-nucleosome complex, and whether this asymmetry is transmitted to the overall nucleosome structure, and therefore also to chromatin, is unclear. Efforts to investigate potential asymmetry due to H1s have been hampered by the DNA sequence, which naturally differs in each gyre. To overcome this issue, we designed and analyzed by cryo-EM a nucleosome reconstituted with a palindromic (601L) 197-bp DNA. As in the non-palindromic 601 sequence, H1 restricts linker DNA flexibility but reveals partial asymmetrical unwrapping. However, in contrast to the non-palindromic nucleosome, in the palindromic nucleosome H1 CTD collapses to the proximal linker. Molecular dynamics simulations show that this could be dictated by a slightly tilted orientation of the globular domain (GD) of H1, which could be linked to the DNA sequence of the nucleosome dyad. Nucleosome dyad determines the H1 C-terminus collapse on distinct DNA arms.,Louro JA, Boopathi R, Beinsteiner B, Mohideen Patel AK, Cheng TC, Angelov D, Hamiche A, Bendar J, Kale S, Klaholz BP, Dimitrov S Structure. 2023 Feb 2;31(2):201-212.e5. doi: 10.1016/j.str.2022.12.005. Epub 2023 , Jan 6. PMID:36610392[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||