1R5M
Crystal Structure Of The C-Terminal WD40 Domain Of Sif2
Summary for 1R5M
| Entry DOI | 10.2210/pdb1r5m/pdb |
| Descriptor | SIR4-interacting protein SIF2, SULFATE ION (3 entities in total) |
| Functional Keywords | transcription corepressor, wd40 repeat, beta propeller, transcription |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Nucleus: P38262 |
| Total number of polymer chains | 1 |
| Total formula weight | 46608.73 |
| Authors | Cerna, D.,Wilson, D.K. (deposition date: 2003-10-10, release date: 2005-03-01, Last modification date: 2024-04-03) |
| Primary citation | Cerna, D.,Wilson, D.K. The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex. J.Mol.Biol., 351:923-935, 2005 Cited by PubMed Abstract: In Saccharomyces cerevisiae, the SIF2 gene product is an integral component of the Set3 complex (SET3C), an assembly of proteins with some homology to the human SMRT and N-CoR corepressor complexes. SET3C has histone deacetylase activity that is responsible for repressing a set of meiotic genes. We have determined the X-ray crystal structure of a 46 kDa C-terminal domain of a SET3C core protein, Sif2p to 1.55 A resolution and a crystallographic R-factor of 19.0%. This domain contains an unusual eight-bladed beta-propeller structure, which differs from other transcriptional corepressor structures such as yeast Tup1p and human groucho (Gro)/TLE1, which have only seven. We have demonstrated intact Sif2p is a tetramer and the N-terminal LisH (Lis-homology)-containing domain mediates tetramerization and interaction with another component of SET3C, Snt1p. Multiple sequence alignments indicate that a surface on the "top" of the protein is conserved among species, suggesting that it may play a common role in binding partner proteins. Since Sif2p appears to be the yeast homolog of human TBL1 and TBLR1, which function in the N-CoR/SMRT complexes, its structural and oligomeric properties are likely to be very similar. PubMed: 16051270DOI: 10.1016/j.jmb.2005.06.025 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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