4LD9

Crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle

4LD9 の概要

• エントリーDOI: 10.2210/pdb4ld9/pdb
• 分子名称: Histone H3.2, Histone H4, Histone H2A, ... (7 entities in total)
• 機能のキーワード: beta barrel, protein-dna complex, double helix, alpha-helix, beta-sheet, double stranded dna, chromatin binding, chromatin, n-terminal acetylation, nucleus, nuclear protein-transcription-dna complex, nuclear protein/transcription/dna
• 由来する生物種: Xenopus laevis (clawed frog,common platanna,platanna); 詳細
• 細胞内の位置: Nucleus: P84233 P62799 P02281 P06701; Nucleus (By similarity): Q6AZJ8
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 269078.93

構造登録者

Arnaudo, N.,Fernandez, I.S.,McLaughlin, S.H.,Peak-Chew, S.Y.,Rhodes, D.,Martino, F. (登録日: 2013-06-24, 公開日: 2013-08-14, 最終更新日: 2024-11-20)

主引用文献

Arnaudo, N.,Fernandez, I.S.,McLaughlin, S.H.,Peak-Chew, S.Y.,Rhodes, D.,Martino, F.
The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.
Nat.Struct.Mol.Biol., 20:1119-1121, 2013

PubMed Abstract: The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.

PubMed: 23934150
DOI: 10.1038/nsmb.2641

実験手法

X-RAY DIFFRACTION (3.306 Å)