8hxx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of the histone deacetylase complex Rpd3S== | |
| + | <StructureSection load='8hxx' size='340' side='right'caption='[[8hxx]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8hxx]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HXX FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ML3:2-{[(2R)-2-AMINO-2-CARBOXYETHYL]SULFANYL}-N,N,N-TRIMETHYLETHANAMINIUM'>ML3</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=8hxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hxx OCA], [https://pdbe.org/8hxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hxx RCSB], [https://www.ebi.ac.uk/pdbsum/8hxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hxx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SIN3_YEAST SIN3_YEAST] Catalytic component of the RPD3 histone deacetylase 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 gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. SIN3 has also a RPD3 independent function required for normal longevity.<ref>PMID:10388812</ref> <ref>PMID:10931932</ref> <ref>PMID:11238941</ref> <ref>PMID:12808094</ref> <ref>PMID:14711989</ref> <ref>PMID:14737171</ref> <ref>PMID:15141165</ref> <ref>PMID:15143171</ref> <ref>PMID:15722108</ref> <ref>PMID:1603074</ref> <ref>PMID:16286008</ref> <ref>PMID:1944290</ref> <ref>PMID:2233725</ref> <ref>PMID:8441414</ref> <ref>PMID:8978024</ref> <ref>PMID:9234741</ref> <ref>PMID:9572144</ref> <ref>PMID:9710596</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Crosstalk between histone modifications represents a fundamental epigenetic mechanism in gene regulation. During the transcription elongation process, the histone deacetylase complex Rpd3S is recruited to H3K36-methylated nucleosomes to suppress cryptic transcription initiation. However, how subunits of Rpd3S are assembled and coordinated to recognize nucleosomal substrates and exert their deacetylation function remains unclear. Here we report the structure of Saccharomyces cerevisiae Rpd3S deacetylase bound to H3K36me3-modified nucleosome at 3.1 A resolution. It shows that Sin3 and Rco1 subunits orchestrate the assembly of the complex and mediate its contact with nucleosome at multiple sites, with the Sin3-DNA interface as a pivotal anchor. The PHD1 domain of Rco1 recognizes the unmodified H3K4 and places the following H3 tail toward the active site of Rpd3, while the chromodomain of Eaf3 subunit recognizes the H3K36me3 mark and contacts both nucleosomal and linker DNA. The second copy of Eaf3-Rco1 is involved in neighboring nucleosome binding. Our work unravels the structural basis of chromatin targeting and deacetylation by the Rpd3S complex. | ||
| - | + | Structure of histone deacetylase complex Rpd3S bound to nucleosome.,Li W, Cui H, Lu Z, Wang H Nat Struct Mol Biol. 2023 Dec;30(12):1893-1901. doi: 10.1038/s41594-023-01121-5. , Epub 2023 Oct 5. PMID:37798513<ref>PMID:37798513</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8hxx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Cui H]] | ||
| + | [[Category: Wang H]] | ||
Current revision
Cryo-EM structure of the histone deacetylase complex Rpd3S
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