8oo9: Difference between revisions

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'''Unreleased structure'''


The entry 8oo9 is ON HOLD
==CryoEM Structure INO80core Hexasome complex ATPase-DNA refinement state1==
<StructureSection load='8oo9' size='340' side='right'caption='[[8oo9]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8oo9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum] 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=8OO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OO9 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8oo9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oo9 OCA], [https://pdbe.org/8oo9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oo9 RCSB], [https://www.ebi.ac.uk/pdbsum/8oo9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oo9 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Loss of H2A-H2B histone dimers is a hallmark of actively transcribed genes, but how the cellular machinery functions in the context of noncanonical nucleosomal particles remains largely elusive. In this work, we report the structural mechanism for adenosine 5'-triphosphate-dependent chromatin remodeling of hexasomes by the INO80 complex. We show how INO80 recognizes noncanonical DNA and histone features of hexasomes that emerge from the loss of H2A-H2B. A large structural rearrangement switches the catalytic core of INO80 into a distinct, spin-rotated mode of remodeling while its nuclear actin module remains tethered to long stretches of unwrapped linker DNA. Direct sensing of an exposed H3-H4 histone interface activates INO80, independently of the H2A-H2B acidic patch. Our findings reveal how the loss of H2A-H2B grants remodelers access to a different, yet unexplored layer of energy-driven chromatin regulation.


Authors:  
Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling.,Zhang M, Jungblut A, Kunert F, Hauptmann L, Hoffmann T, Kolesnikova O, Metzner F, Moldt M, Weis F, DiMaio F, Hopfner KP, Eustermann S Science. 2023 Jul 21;381(6655):313-319. doi: 10.1126/science.adf6287. Epub 2023 , Jun 29. PMID:37384673<ref>PMID:37384673</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8oo9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chaetomium thermophilum]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Eustermann S]]
[[Category: Hoffmann T]]
[[Category: Jungblut A]]
[[Category: Zhang M]]

Latest revision as of 15:40, 26 July 2023

CryoEM Structure INO80core Hexasome complex ATPase-DNA refinement state1CryoEM Structure INO80core Hexasome complex ATPase-DNA refinement state1

Structural highlights

8oo9 is a 3 chain structure with sequence from Chaetomium thermophilum and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Loss of H2A-H2B histone dimers is a hallmark of actively transcribed genes, but how the cellular machinery functions in the context of noncanonical nucleosomal particles remains largely elusive. In this work, we report the structural mechanism for adenosine 5'-triphosphate-dependent chromatin remodeling of hexasomes by the INO80 complex. We show how INO80 recognizes noncanonical DNA and histone features of hexasomes that emerge from the loss of H2A-H2B. A large structural rearrangement switches the catalytic core of INO80 into a distinct, spin-rotated mode of remodeling while its nuclear actin module remains tethered to long stretches of unwrapped linker DNA. Direct sensing of an exposed H3-H4 histone interface activates INO80, independently of the H2A-H2B acidic patch. Our findings reveal how the loss of H2A-H2B grants remodelers access to a different, yet unexplored layer of energy-driven chromatin regulation.

Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling.,Zhang M, Jungblut A, Kunert F, Hauptmann L, Hoffmann T, Kolesnikova O, Metzner F, Moldt M, Weis F, DiMaio F, Hopfner KP, Eustermann S Science. 2023 Jul 21;381(6655):313-319. doi: 10.1126/science.adf6287. Epub 2023 , Jun 29. PMID:37384673[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Zhang M, Jungblut A, Kunert F, Hauptmann L, Hoffmann T, Kolesnikova O, Metzner F, Moldt M, Weis F, DiMaio F, Hopfner KP, Eustermann S. Hexasome-INO80 complex reveals structural basis of noncanonical nucleosome remodeling. Science. 2023 Jul 21;381(6655):313-319. PMID:37384673 doi:10.1126/science.adf6287

8oo9, resolution 3.20Å

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