5B0Y

Crystal structure of the nucleosome containing histone H3 with the crotonylated lysine 122

5B0Y の概要

• エントリーDOI: 10.2210/pdb5b0y/pdb
• 関連するPDBエントリー: 5B0Z
• 分子名称: Histone H3.2, Histone H4, Histone H2A type 1-B/E, ... (8 entities in total)
• 機能のキーワード: histone modification, nucleosome, dna binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 202278.55

構造登録者

Suzuki, Y.,Horikoshi, N.,Kurumizaka, H. (登録日: 2015-11-13, 公開日: 2016-01-27, 最終更新日: 2023-11-15)

主引用文献

Suzuki, Y.,Horikoshi, N.,Kato, D.,Kurumizaka, H.
Crystal structure of the nucleosome containing histone H3 with crotonylated lysine 122
Biochem.Biophys.Res.Commun., 469:483-489, 2016

PubMed Abstract: The crotonylation of histones is an important post-translational modification, and epigenetically functions in the regulation of genomic DNA activity. The histone modifications in the structured "histone-fold" domains are considered to have an especially important impact on the nucleosome structure and dynamics. In the present study, we reconstituted the human nucleosome containing histone H3.2 crotonylated at the Lys122 residue, and determined its crystal structure at 2.56 Å resolution. We found that the crotonylation of the H3 Lys122 residue does not affect the overall nucleosome structure, but locally impedes the formation of the water-mediated hydrogen bond with the DNA backbone. Consistently, thermal stability assays revealed that the H3 Lys122 crotonylation, as well as the H3 Lys122 acetylation, clearly reduced the histone-DNA association.

PubMed: 26694698
DOI: 10.1016/j.bbrc.2015.12.041

実験手法

X-RAY DIFFRACTION (2.557 Å)