5tdw

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<StructureSection load='5tdw' size='340' side='right'caption='[[5tdw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='5tdw' size='340' side='right'caption='[[5tdw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tdw]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TDW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TDW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tdw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [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=5TDW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TDW 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=NA:SODIUM+ION'>NA</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]] 1.7&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tdr|5tdr]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5tdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdw OCA], [https://pdbe.org/5tdw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tdw RCSB], [https://www.ebi.ac.uk/pdbsum/5tdw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdw ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5tdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tdw OCA], [http://pdbe.org/5tdw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tdw RCSB], [http://www.ebi.ac.uk/pdbsum/5tdw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tdw ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SET3_YEAST SET3_YEAST]] Transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. Required for both gene activation and repression. Part of the Set3C complex, which is required to repress early/middle sporulation genes during meiosis. Required for the transcriptional activation of genes with high activity.<ref>PMID:12434058</ref>
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[https://www.uniprot.org/uniprot/SET3_YEAST SET3_YEAST] Transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. Required for both gene activation and repression. Part of the Set3C complex, which is required to repress early/middle sporulation genes during meiosis. Required for the transcriptional activation of genes with high activity.<ref>PMID:12434058</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The plant homeodomain (PHD) finger of Set3 binds methylated lysine 4 of histone H3 in vitro and in vivo; however, precise selectivity of this domain has not been fully characterized. Here, we explore the determinants of methyllysine recognition by the PHD fingers of Set3 and its orthologs. We use X-ray crystallographic and spectroscopic approaches to show that the Set3 PHD finger binds di- and trimethylated states of H3K4 with comparable affinities and employs similar molecular mechanisms to form complexes with either mark. Composition of the methyllysine-binding pocket plays an essential role in determining the selectivity of the PHD fingers. The finding that the histone-binding activity is not conserved in the PHD finger of Set4 suggests different functions for the Set3 and Set4 paralogs.
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Structural Insight into Recognition of Methylated Histone H3K4 by Set3.,Gatchalian J, Ali M, Andrews FH, Zhang Y, Barrett AS, Kutateladze TG J Mol Biol. 2016 Sep 30. pii: S0022-2836(16)30400-4. doi:, 10.1016/j.jmb.2016.09.020. PMID:27697561<ref>PMID:27697561</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 5tdw" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ali, M]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Andrews, F H]]
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[[Category: Ali M]]
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[[Category: Kutateladze, T G]]
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[[Category: Andrews FH]]
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[[Category: Epigenetic]]
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[[Category: Kutateladze TG]]
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[[Category: Histone]]
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[[Category: Methylation]]
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[[Category: Transcription]]
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Revision as of 15:40, 6 March 2024

Set3 PHD finger in complex with histone H3K4me3

PDB ID 5tdw

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