3E9G

Crystal structure long-form (residue1-124) of Eaf3 chromo domain

3E9G の概要

• エントリーDOI: 10.2210/pdb3e9g/pdb
• 関連するPDBエントリー: 3E9F
• 分子名称: Chromatin modification-related protein EAF3 (2 entities in total)
• 機能のキーワード: chromatin remodeling, eaf3, chromo domain, transcription factor, transcription regulation, chromatin regulator, dna damage, dna repair, nucleus, transcription
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Nucleus : Q12432
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30184.25

構造登録者

Sun, B.,Hong, J.,Zhang, P.,Lin, D.,Ding, J. (登録日: 2008-08-22, 公開日: 2008-11-04, 最終更新日: 2023-11-01)

主引用文献

Sun, B.,Hong, J.,Zhang, P.,Dong, X.,Shen, X.,Lin, D.,Ding, J.
Molecular Basis of the Interaction of Saccharomyces cerevisiae Eaf3 Chromo Domain with Methylated H3K36
J.Biol.Chem., 283:36504-36512, 2008

PubMed Abstract: Eaf3 is a component of both NuA4 histone acetyltransferase and Rpd3S histone deacetylase complexes in Saccharomyces cerevisiae. It is involved in the regulation of the global pattern of histone acetylation that distinguishes promoters from coding regions. Eaf3 contains a chromo domain at the N terminus that can bind to methylated Lys-36 of histone H3 (H3K36). We report here the crystal structures of the Eaf3 chromo domain in two truncation forms. Unlike the typical HP1 and Polycomb chromo domains, which contain a large groove to bind the modified histone tail, the Eaf3 chromo domain assumes an autoinhibited chromo barrel domain similar to the human MRG15 chromo domain. Compared with other chromo domains, the Eaf3 chromo domain contains a unique 38-residue insertion that folds into two short beta-strands and a long flexible loop to flank the beta-barrel core. Both isothermal titration calorimetry and surface plasmon resonance studies indicate that the interaction between the Eaf3 chromo domain and the trimethylated H3K36 peptide is relatively weak, with a K(D) of approximately 10(-4) m. NMR titration studies demonstrate that the methylated H3K36 peptide is bound to the cleft formed by the C-terminal alpha-helix and the beta-barrel core. Site-directed mutagenesis study and in vitro binding assay results show that the conserved aromatic residues Tyr-23, Tyr-81, Trp-84, and Trp-88, which form a hydrophobic pocket at one end of the beta-barrel, are essential for the binding of the methylated H3K36. These results reveal the molecular mechanism of the recognition and binding of the methylated H3K36 by Eaf3 and provide new insights into the functional roles of the Eaf3 chromo domain.

PubMed: 18984594
DOI: 10.1074/jbc.M806564200

実験手法

X-RAY DIFFRACTION (2.5 Å)