3MP8
Crystal structure of Sgf29 tudor domain
3MP8 の概要
エントリーDOI | 10.2210/pdb3mp8/pdb |
関連するPDBエントリー | 3MP1 3MP6 |
関連するBIRD辞書のPRD_ID | PRD_900001 |
分子名称 | Maltose-binding periplasmic protein,LINKER,SAGA-associated factor 29, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, GLYCEROL, ... (8 entities in total) |
機能のキーワード | histone, tudor domain, saga, histone binding protein |
由来する生物種 | Escherichia coli K-12 詳細 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 59714.77 |
構造登録者 | |
主引用文献 | Bian, C.,Xu, C.,Ruan, J.,Lee, K.K.,Burke, T.L.,Tempel, W.,Barsyte, D.,Li, J.,Wu, M.,Zhou, B.O.,Fleharty, B.E.,Paulson, A.,Allali-Hassani, A.,Zhou, J.Q.,Mer, G.,Grant, P.A.,Workman, J.L.,Zang, J.,Min, J. Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation Embo J., 30:2829-2842, 2011 Cited by PubMed Abstract: The SAGA (Spt-Ada-Gcn5 acetyltransferase) complex is an important chromatin modifying complex that can both acetylate and deubiquitinate histones. Sgf29 is a novel component of the SAGA complex. Here, we report the crystal structures of the tandem Tudor domains of Saccharomyces cerevisiae and human Sgf29 and their complexes with H3K4me2 and H3K4me3 peptides, respectively, and show that Sgf29 selectively binds H3K4me2/3 marks. Our crystal structures reveal that Sgf29 harbours unique tandem Tudor domains in its C-terminus. The tandem Tudor domains in Sgf29 tightly pack against each other face-to-face with each Tudor domain harbouring a negatively charged pocket accommodating the first residue alanine and methylated K4 residue of histone H3, respectively. The H3A1 and K4me3 binding pockets and the limited binding cleft length between these two binding pockets are the structural determinants in conferring the ability of Sgf29 to selectively recognize H3K4me2/3. Our in vitro and in vivo functional assays show that Sgf29 recognizes methylated H3K4 to recruit the SAGA complex to its targets sites and mediates histone H3 acetylation, underscoring the importance of Sgf29 in gene regulation. PubMed: 21685874DOI: 10.1038/emboj.2011.193 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.92 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード