1r5m
From Proteopedia
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Crystal Structure Of The C-Terminal WD40 Domain Of Sif2
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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