1R5M

Crystal Structure Of The C-Terminal WD40 Domain Of Sif2

1R5M の概要

• エントリーDOI: 10.2210/pdb1r5m/pdb
• 分子名称: SIR4-interacting protein SIF2, SULFATE ION (3 entities in total)
• 機能のキーワード: transcription corepressor, wd40 repeat, beta propeller, transcription
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P38262
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 46608.73

構造登録者

Cerna, D.,Wilson, D.K. (登録日: 2003-10-10, 公開日: 2005-03-01, 最終更新日: 2024-04-03)

主引用文献

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

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: 16051270
DOI: 10.1016/j.jmb.2005.06.025

実験手法

X-RAY DIFFRACTION (1.55 Å)