3TIX
Crystal structure of the Chp1-Tas3 complex core
Summary for 3TIX
| Entry DOI | 10.2210/pdb3tix/pdb |
| Descriptor | Ubiquitin-like protein SMT3,RNA-induced transcriptional silencing complex protein tas3, Chromo domain-containing protein 1, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | pin, rossmann fold, spoc, alpha-helical hairpin, heterochromatin, silencing, rits, rnai, argonaute, clrc, rdrc, nucleus, gene regulation-protein binding complex, gene regulation/protein binding |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Nucleus: O94687 Q10103 |
| Total number of polymer chains | 4 |
| Total formula weight | 151790.99 |
| Authors | Schalch, T.,Joshua-Tor, L. (deposition date: 2011-08-22, release date: 2011-11-16, Last modification date: 2024-02-28) |
| Primary citation | Schalch, T.,Job, G.,Shanker, S.,Partridge, J.F.,Joshua-Tor, L. The Chp1-Tas3 core is a multifunctional platform critical for gene silencing by RITS. Nat.Struct.Mol.Biol., 18:1351-1357, 2011 Cited by PubMed Abstract: RNA interference (RNAi) is critical for the assembly of heterochromatin at Schizosaccharomyces pombe centromeres. Central to this process is the RNA-induced initiation of transcriptional gene silencing (RITS) complex, which physically anchors small noncoding RNAs to chromatin. RITS includes Ago1, the chromodomain protein Chp1, and Tas3, which forms a bridge between Chp1 and Ago1. Chp1 is a large protein with no recognizable domains, apart from its chromodomain. Here we describe how the structured C-terminal half of Chp1 binds the Tas3 N-terminal domain, revealing the tight association of Chp1 and Tas3. The structure also shows a PIN domain at the C-terminal tip of Chp1 that controls subtelomeric transcripts through a post-transcriptional mechanism. We suggest that the Chp1-Tas3 complex provides a solid and versatile platform to recruit both RNAi-dependent and RNAi-independent gene-silencing pathways for locus-specific regulation of heterochromatin. PubMed: 22081013DOI: 10.1038/nsmb.2151 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9001 Å) |
Structure validation
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