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8a5a: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8a5a]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A5A FirstGlance]. <br>
<table><tr><td colspan='2'>[[8a5a]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8A5A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8A5A FirstGlance]. <br>
</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=END:1,6 5,9 8,12 11,16-TETRAANHYDRO-2,3,4,10,13,14-HEXADEOXY-D-GLYCERO-D-ALLO-D-GULO-HEPTADECA-2,13-DIENITOL'>END</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#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=8a5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a5a OCA], [https://pdbe.org/8a5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a5a RCSB], [https://www.ebi.ac.uk/pdbsum/8a5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a5a ProSAT]</span></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=8a5a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8a5a OCA], [https://pdbe.org/8a5a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8a5a RCSB], [https://www.ebi.ac.uk/pdbsum/8a5a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8a5a ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/INO80_YEAST INO80_YEAST] ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair (PubMed:10952318, PubMed:12887900). Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates (PubMed:10952318, PubMed:10361278). The INO80 complex is involved in DNA repair by associating with 'Ser-129' phosphorylated H2A histones as a response to DNA damage (PubMed:15607974, PubMed:15607975).<ref>PMID:10361278</ref> <ref>PMID:10952318</ref> <ref>PMID:12887900</ref> <ref>PMID:15607974</ref> <ref>PMID:15607975</ref>  
[https://www.uniprot.org/uniprot/IES4_YEAST IES4_YEAST]  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The nucleosomal landscape of chromatin depends on the concerted action of chromatin remodelers. The INO80 remodeler specifically places nucleosomes at the boundary of gene regulatory elements, which is proposed to be the result of an ATP-dependent nucleosome sliding activity that is regulated by extranucleosomal DNA features. Here, we use cryo-electron microscopy and functional assays to reveal how INO80 binds and is regulated by extranucleosomal DNA. Structures of the regulatory A-module bound to DNA clarify the mechanism of linker DNA binding. The A-module is connected to the motor unit via an HSA/post-HSA lever element to chemomechanically couple the motor and linker DNA sensing. Two notable sites of curved DNA recognition by coordinated action of the four actin/actin-related proteins and the motor suggest how sliding by INO80 can be regulated by extranucleosomal DNA features. Last, the structures clarify the recruitment of YY1/Ies4 subunits and reveal deep architectural similarities between the regulatory modules of INO80 and SWI/SNF complexes.
 
Structural mechanism of extranucleosomal DNA readout by the INO80 complex.,Kunert F, Metzner FJ, Jung J, Hopfler M, Woike S, Schall K, Kostrewa D, Moldt M, Chen JX, Bantele S, Pfander B, Eustermann S, Hopfner KP Sci Adv. 2022 Dec 9;8(49):eadd3189. doi: 10.1126/sciadv.add3189. Epub 2022 Dec 9. PMID:36490333<ref>PMID:36490333</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8a5a" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

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