5IKJ
Structure of Clr2 bound to the Clr1 C-terminus
Summary for 5IKJ
| Entry DOI | 10.2210/pdb5ikj/pdb |
| Descriptor | Cryptic loci regulator 2, Cryptic loci regulator protein 1, ZINC ION, ... (5 entities in total) |
| Functional Keywords | methyl-cpg-binding domain, bah domain, chromobarrel domain, complex, cell cycle, transcription |
| Biological source | Schizosaccharomyces pombe 972h- (Fission yeast) More |
| Cellular location | Nucleus : O13881 O74808 |
| Total number of polymer chains | 2 |
| Total formula weight | 72974.95 |
| Authors | Pfister, Y.,Schalch, T. (deposition date: 2016-03-03, release date: 2016-04-20, Last modification date: 2024-05-08) |
| Primary citation | Job, G.,Brugger, C.,Xu, T.,Lowe, B.R.,Pfister, Y.,Qu, C.,Shanker, S.,Banos Sanz, J.I.,Partridge, J.F.,Schalch, T. SHREC Silences Heterochromatin via Distinct Remodeling and Deacetylation Modules. Mol.Cell, 62:207-221, 2016 Cited by PubMed Abstract: 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. PubMed: 27105116DOI: 10.1016/j.molcel.2016.03.016 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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