7qce

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7qce]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phoenix_dactylifera Phoenix dactylifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QCE FirstGlance]. <br>
<table><tr><td colspan='2'>[[7qce]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phoenix_dactylifera Phoenix dactylifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QCE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QCE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7qce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qce OCA], [https://pdbe.org/7qce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qce RCSB], [https://www.ebi.ac.uk/pdbsum/7qce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qce 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=7qce FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qce OCA], [https://pdbe.org/7qce PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qce RCSB], [https://www.ebi.ac.uk/pdbsum/7qce PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qce ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A8B7MWH5_PHODC A0A8B7MWH5_PHODC]
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PHD fingers are modular domains in chromatin-associated proteins that decode the methylation status of histone H3 tails. A PHD finger signature is found in plant vernalization (VEL) proteins, which function as accessory factors of the Polycomb system to control flowering in Arabidopsis through an epigenetic silencing mechanism. It has been proposed that VEL PHD fingers bind to methylated histone H3 tails to facilitate association of the Polycomb silencing machinery with target genes. Here, we use structural analysis by X-ray crystallography to show that the VEL PHD finger forms the central module of a larger compact tripartite superdomain that also contains a zinc finger and a four-helix bundle. This PHD superdomain fold is only found in one other family, the OBERON proteins, which have multiple functions in Arabidopsis meristems to control plant growth. The putative histone-binding surface of OBERON proteins exhibits the characteristic three-pronged pocket of histone-binding PHD fingers and binds to methylated histone H3 tails. However, that of VEL PHD fingers lacks this architecture and exhibits unusually high positive surface charge. This VEL PHD superdomain neither binds to unmodified nor variously modified histone H3 tails, as demonstrated by isothermal calorimetry and NMR spectroscopy. Instead, the VEL PHD superdomain interacts with negatively charged polymers. Our evidence argues for evolution of a divergent function for the PHD superdomain in vernalization that does not involve histone tail decoding.
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Plant vernalization proteins contain unusual PHD superdomains without histone H3 binding activity.,Franco-Echevarria E, Rutherford TJ, Fiedler M, Dean C, Bienz M J Biol Chem. 2022 Sep 27;298(11):102540. doi: 10.1016/j.jbc.2022.102540. PMID:36174674<ref>PMID:36174674</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7qce" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Crystal structure of an atypical PHD finger of VIN3

PDB ID 7qce

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OCA

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