5ikf
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the C-terminal domain of the Mit1 nucleosome remodeler in complex with Clr1== | |
| + | <StructureSection load='5ikf' size='340' side='right'caption='[[5ikf]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ikf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IKF FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5ikf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ikf OCA], [https://pdbe.org/5ikf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ikf RCSB], [https://www.ebi.ac.uk/pdbsum/5ikf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ikf ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MIT1_SCHPO MIT1_SCHPO] Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).<ref>PMID:17289569</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nucleosome remodeling and deacetylation (NuRD) complexes are co-transcriptional regulators implicated in differentiation, development, and diseases. Methyl-CpG binding domain (MBD) proteins play an essential role in recruitment of NuRD complexes to their target sites in chromatin. The related SHREC complex in fission yeast drives transcriptional gene silencing in heterochromatin through cooperation with HP1 proteins. How remodeler and histone deacetylase (HDAC) cooperate within NuRD complexes remains unresolved. We determined that in SHREC the two modules occupy distant sites on the scaffold protein Clr1 and that repressive activity of SHREC can be modulated by the expression level of the HDAC-associated Clr1 domain alone. Moreover, the crystal structure of Clr2 reveals an MBD-like domain mediating recruitment of the HDAC module to heterochromatin. Thus, SHREC bi-functionality is organized in two separate modules with separate recruitment mechanisms, which work together to elicit transcriptional silencing at heterochromatic loci. | ||
| - | + | SHREC Silences Heterochromatin via Distinct Remodeling and Deacetylation Modules.,Job G, Brugger C, Xu T, Lowe BR, Pfister Y, Qu C, Shanker S, Banos Sanz JI, Partridge JF, Schalch T Mol Cell. 2016 Apr 21;62(2):207-21. doi: 10.1016/j.molcel.2016.03.016. PMID:27105116<ref>PMID:27105116</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Brugger | + | <div class="pdbe-citations 5ikf" style="background-color:#fffaf0;"></div> |
| - | [[Category: Schalch | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Schizosaccharomyces pombe 972h-]] | ||
| + | [[Category: Brugger C]] | ||
| + | [[Category: Schalch T]] | ||
Current revision
Crystal structure of the C-terminal domain of the Mit1 nucleosome remodeler in complex with Clr1
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