8oot: Difference between revisions

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-'''Unreleased structure'''
-The entry 8oot is ON HOLD
+==CryoEM Structure INO80core Hexasome complex Arp5 Ies6 refinement state2==
+<StructureSection load='8oot' size='340' side='right'caption='[[8oot]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8oot]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OOT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OOT 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]] 2.85&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=8oot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8oot OCA], [https://pdbe.org/8oot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8oot RCSB], [https://www.ebi.ac.uk/pdbsum/8oot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8oot ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/G0S590_CHATD G0S590_CHATD]
+<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 8oot" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Chaetomium thermophilum]]
+[[Category: Large Structures]]
+[[Category: Eustermann S]]
+[[Category: Hoffmann T]]
+[[Category: Jungblut A]]
+[[Category: Zhang M]]