5wle

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m (Protected "5wle" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5wle is ON HOLD until Paper Publication
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==Crystal structure of the PPS PHD finger in complex with H3K4me3==
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<StructureSection load='5wle' size='340' side='right' caption='[[5wle]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5wle]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WLE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WLE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wle OCA], [http://pdbe.org/5wle PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wle RCSB], [http://www.ebi.ac.uk/pdbsum/5wle PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wle ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The protein partner of Sans-fille (PPS) and its human homolog DIDO mediate diverse chromatin activities, including the regulation of stemness genes in embryonic stem cells and splicing in Drosophila. Here, we show that the PHD fingers of PPS and DIDO recognize the histone mark H3K4me3 in a pH-dependent manner: the binding is enhanced at high pH values but is decreased at low pH. Structural analysis reveals that the pH dependency is due to the presence of a histidine residue in the K4me3-binding aromatic cage of PPS. The pH-dependent mechanism is conserved in DIDO but is lost in yeast Bye1. Acidification of cells leads to the accelerated efflux of endogenous DIDO, indicating the pH-dependent sensing of H3K4me3 in vivo. This novel mode for the recognition of H3K4me3 establishes the PHD fingers of PPS and DIDO as unique epigenetic readers and high pH sensors and suggests a role for the histidine switch during mitosis.
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Authors:
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A Unique pH-Dependent Recognition of Methylated Histone H3K4 by PPS and DIDO.,Tencer AH, Gatchalian J, Klein BJ, Khan A, Zhang Y, Strahl BD, van Wely KHM, Kutateladze TG Structure. 2017 Sep 8. pii: S0969-2126(17)30262-9. doi:, 10.1016/j.str.2017.08.009. PMID:28919441<ref>PMID:28919441</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5wle" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Klein, B J]]
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[[Category: Kutateladze, T G]]
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[[Category: Epigenetic]]
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[[Category: Histone]]
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[[Category: Hydrolase]]
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[[Category: Phd]]
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[[Category: Trimethylated]]

Revision as of 09:10, 4 October 2017

Crystal structure of the PPS PHD finger in complex with H3K4me3

5wle, resolution 1.95Å

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