3AYW

Crystal Structure of Human Nucleosome Core Particle Containing H3K56Q mutation

3AYW の概要

• エントリーDOI: 10.2210/pdb3ayw/pdb
• 関連するPDBエントリー: 3AFA
• 分子名称: Histone H3.1, Histone H4, Histone H2A type 1-B/E, ... (7 entities in total)
• 機能のキーワード: histone-fold, nucleosome, structural protein-dna complex, structural protein/dna
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P68431 P62805 P04908 P06899
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 202974.72

構造登録者

Iwasaki, W.,Tachiwana, H.,Kawaguchi, K.,Shibata, T.,Kagawa, W.,Kurumizaka, H. (登録日: 2011-05-19, 公開日: 2011-09-21, 最終更新日: 2023-11-01)

主引用文献

Iwasaki, W.,Tachiwana, H.,Kawaguchi, K.,Shibata, T.,Kagawa, W.,Kurumizaka, H.
Comprehensive Structural Analysis of Mutant Nucleosomes Containing Lysine to Glutamine (KQ) Substitutions in the H3 and H4 Histone-Fold Domains
Biochemistry, 50:7822-7832, 2011

PubMed Abstract: Post-translational modifications (PTMs) of histones play important roles in regulating the structure and function of chromatin in eukaryotes. Although histone PTMs were considered to mainly occur at the N-terminal tails of histones, recent studies have revealed that PTMs also exist in the histone-fold domains, which are commonly shared among the core histones H2A, H2B, H3, and H4. The lysine residue is a major target for histone PTM, and the lysine to glutamine (KQ) substitution is known to mimic the acetylated states of specific histone lysine residues in vivo. Human histones H3 and H4 contain 11 lysine residues in their histone-fold domains (five for H3 and six for H4), and eight of these lysine residues are known to be targets for acetylation. In the present study, we prepared 11 mutant nucleosomes, in which each of the lysine residues of the H3 and H4 histone-fold domains was replaced by glutamine: H3 K56Q, H3 K64Q, H3 K79Q, H3 K115Q, H3 K122Q, H4 K31Q, H4 K44Q, H4 K59Q, H4 K77Q, H4 K79Q, and H4 K91Q. The crystal structures of these mutant nucleosomes were determined at 2.4-3.5 Å resolutions. Some of these amino acid substitutions altered the local protein-DNA interactions and the interactions between amino acid residues within the nucleosome. Interestingly, the C-terminal region of H2A was significantly disordered in the nucleosome containing H4 K44Q. These results provide an important structural basis for understanding how histone modifications and mutations affect chromatin structure and function.

PubMed: 21812398
DOI: 10.1021/bi201021h

実験手法

X-RAY DIFFRACTION (2.9 Å)