1Q17

Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide

1Q17 の概要

• エントリーDOI: 10.2210/pdb1q17/pdb
• 関連するPDBエントリー: 1Q14
• 分子名称: HST2 protein, ZINC ION, CHLORIDE ION, ... (5 entities in total)
• 機能のキーワード: histone deacetylase, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus (Potential): P53686
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 103445.18

構造登録者

Zhao, K.,Chai, X.,Marmorstein, R. (登録日: 2003-07-18, 公開日: 2003-11-18, 最終更新日: 2023-08-16)

主引用文献

Zhao, K.,Chai, X.,Marmorstein, R.
Structure of the Yeast Hst2 Protein Deacetylase in Ternary Complex with 2'-O-Acetyl ADP Ribose and Histone Peptide.
Structure, 11:1403-1411, 2003

PubMed Abstract: Sir2 proteins are NAD(+)-dependant protein deactylases that have been implicated in playing roles in gene silencing, DNA repair, genome stability, longevity, metabolism, and cell physiology. To define the mechanism of Sir2 activity, we report the 1.5 A crystal structure of the yeast Hst2 (yHst2) Sir2 protein in ternary complex with 2'-O-acetyl ADP ribose and an acetylated histone H4 peptide. The structure captures both ligands meeting within an enclosed tunnel between the small and large domains of the catalytic protein core and permits the assignment of a detailed catalytic mechanism for the Sir2 proteins that is consistent with solution and enzymatic studies. Comparison of the ternary complex with the yHst2/NAD(+) complex, also reported here, and nascent yHst2 structure also reveals that NAD(+) binding accompanies intramolecular loop rearrangement for more stable NAD(+) and acetyl-lysine binding, and that acetyl-lysine peptide binding induces a trimer-monomer protein transition involving nonconserved Sir2 residues.

PubMed: 14604530
DOI: 10.1016/j.str.2003.09.016

実験手法

X-RAY DIFFRACTION (2.7 Å)