3C9C

Structural Basis of Histone H4 Recognition by p55

3C9C の概要

• エントリーDOI: 10.2210/pdb3c9c/pdb
• 関連するPDBエントリー: 3C99
• 分子名称: Chromatin assembly factor 1 p55 subunit, Histone H4, 27-residue peptide, CADMIUM ION (3 entities in total)
• 機能のキーワード: p55, chromatin, epigenetics, wd4, histone, chromatin regulator, nucleus, phosphoprotein, repressor, transcription, transcription regulation, wd repeat, chromosomal protein, dna-binding, nucleosome core, nuclear protein, transcription repressor
• 由来する生物種: Drosophila melanogaster (fruit fly); 詳細
• 細胞内の位置: Nucleus: Q24572 P84040
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52796.44

構造登録者

Song, J.J.,Garlick, J.D.,Kingston, R.E. (登録日: 2008-02-15, 公開日: 2008-05-13, 最終更新日: 2023-08-30)

主引用文献

Song, J.J.,Garlick, J.D.,Kingston, R.E.
Structural basis of histone H4 recognition by p55.
Genes Dev., 22:1313-1318, 2008

PubMed Abstract: p55 is a common component of many chromatin-modifying complexes and has been shown to bind to histones. Here, we present a crystal structure of Drosophila p55 bound to a histone H4 peptide. p55, a predicted WD40 repeat protein, recognizes the first helix of histone H4 via a binding pocket located on the side of a beta-propeller structure. The pocket cannot accommodate the histone fold of H4, which must be altered to allow p55 binding. Reconstitution experiments show that the binding pocket is important to the function of p55-containing complexes. These data demonstrate that WD40 repeat proteins use various surfaces to direct the modification of histones.

PubMed: 18443147
DOI: 10.1101/gad.1653308

実験手法

X-RAY DIFFRACTION (3.2 Å)