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3MP8

Crystal structure of Sgf29 tudor domain

3MP8 の概要
エントリーDOI10.2210/pdb3mp8/pdb
関連するPDBエントリー3MP1 3MP6
関連するBIRD辞書のPRD_IDPRD_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
Li, J.,Wu, M.,Ruan, J.,Zang, J. (登録日: 2010-04-26, 公開日: 2011-05-04, 最終更新日: 2023-11-01)
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: 21685874
DOI: 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
Validation report summary of 3mp8
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-06に公開中

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