7yi4

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'''Unreleased structure'''
 
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The entry 7yi4 is ON HOLD until Paper Publication
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==Cryo-EM structure of Rpd3S complex bound to H3K36me3 nucleosome in close state==
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<StructureSection load='7yi4' size='340' side='right'caption='[[7yi4]], [[Resolution|resolution]] 3.96&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7yi4]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C], [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=7YI4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YI4 FirstGlance]. <br>
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Description:
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.96&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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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=ZN:ZINC+ION'>ZN</scene></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=7yi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yi4 OCA], [https://pdbe.org/7yi4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yi4 RCSB], [https://www.ebi.ac.uk/pdbsum/7yi4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yi4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RPD3_YEAST RPD3_YEAST] Catalytic component of the RPD3 histone deacetylase (HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events. Is involved in rDNA and telomere silencing and in double strand breaks repair. Required for both full transcription repression and activation of many genes including cell type-specific genes (STE6, TY2 and HO), cell differentiation-specific genes (SPO13), genes that respond to external signals (PHO5) and TRK2. The RPD3 complexes regulate also chromosomal replication timing.<ref>PMID:10079324</ref> <ref>PMID:10359799</ref> <ref>PMID:10388812</ref> <ref>PMID:10931932</ref> <ref>PMID:11069890</ref> <ref>PMID:12089521</ref> <ref>PMID:12192044</ref> <ref>PMID:12808094</ref> <ref>PMID:14711989</ref> <ref>PMID:14737171</ref> <ref>PMID:15141165</ref> <ref>PMID:15143171</ref> <ref>PMID:15456858</ref> <ref>PMID:16286008</ref> <ref>PMID:1944291</ref> <ref>PMID:8962081</ref> <ref>PMID:8978024</ref> <ref>PMID:9512514</ref> <ref>PMID:9710596</ref>
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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: Large Structures]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Synthetic construct]]
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[[Category: Xenopus laevis]]
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[[Category: Guan HP]]
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[[Category: Li HT]]
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[[Category: Wang P]]
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[[Category: Yan CY]]

Current revision

Cryo-EM structure of Rpd3S complex bound to H3K36me3 nucleosome in close state

PDB ID 7yi4

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