1r5m | pdb_00001r5m
Crystal Structure Of The C-Terminal WD40 Domain Of Sif2
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Overview
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.
About this Structure
1R5M is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex., Cerna D, Wilson DK, J Mol Biol. 2005 Aug 26;351(4):923-35. PMID:16051270
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