8eu2: Difference between revisions

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-'''Unreleased structure'''
-The entry 8eu2 is ON HOLD  until Paper Publication
+==Class3 of the INO80-Hexasome complex==
+<StructureSection load='8eu2' size='340' side='right'caption='[[8eu2]], [[Resolution|resolution]] 2.93&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8eu2]] is a 8 chain structure with sequence from [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=8EU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EU2 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]] 2.93&#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=8eu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eu2 OCA], [https://pdbe.org/8eu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eu2 RCSB], [https://www.ebi.ac.uk/pdbsum/8eu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eu2 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/H3C_XENLA H3C_XENLA] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of S. cerevisiae INO80 bound to a hexasome or a nucleosome. INO80 binds the two substrates in substantially different orientations. On a hexasome, INO80 places its ATPase subunit, Ino80, at superhelical location (SHL)-2, across from SHL-6/-7 as previously seen on nucleosomes. Our results suggest that INO80 action on hexasomes resembles action by other remodelers on nucleosomes, such that Ino80 is maximally active near SHL-2. The SHL-2 position also plays a critical role for nucleosome remodeling by INO80. Overall, the mechanistic adaptations used by INO80 for preferential hexasome sliding imply that sub-nucleosomal particles play considerable regulatory roles.
-Authors:
+Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility.,Wu H, Munoz EN, Hsieh LJ, Chio US, Gourdet MA, Narlikar GJ, Cheng Y Science. 2023 Jun 28. doi: 10.1126/science.adf4197. PMID:37384669<ref>PMID:37384669</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 8eu2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Synthetic construct]]
+[[Category: Xenopus laevis]]
+[[Category: Cheng YF]]
+[[Category: Gourdet M]]
+[[Category: Munoz E]]
+[[Category: Narlikar G]]
+[[Category: Wu H]]