2ZFN

Self-acetylation mediated histone H3 lysine 56 acetylation by rtt109

2ZFN の概要

• エントリーDOI: 10.2210/pdb2zfn/pdb
• 関連するPDBエントリー: 2RIM
• 分子名称: Regulator of Ty1 transposition protein 109, ACETYL COENZYME *A, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: histone h3 lysine 56 acetylation, dna damage, dna repair, nucleus, transcription, transcription regulation, transferase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Nucleus: Q07794
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 53963.77

構造登録者

Yuan, Y.A. (登録日: 2008-01-08, 公開日: 2008-09-23, 最終更新日: 2024-11-20)

主引用文献

Lin, C.,Yuan, Y.A.
Structural insights into histone h3 lysine 56 acetylation by rtt109
Structure, 16:1503-1510, 2008

PubMed Abstract: Histone acetylation plays important roles for the regulation of many fundamental cellular processes. Saccharomyces cerevisiae Rtt109 is an important class of histone acetyltransferases (HATs), which promote genome stability by directly acetylating newly synthesized histone H3 lysine 56 (H3-K56) through an unknown mechanism. Here, we report the crystal structures of Rtt109 at 2.2 A and Rtt109/Acetyl-CoA binary complex at 1.9 A. The structure displays a vise-like topology with mixed three-layered alpha/beta module forming the central module, whose core region resembles the structure of GCN5 HAT domain and P300/CBP HAT domain. Using structural and biochemical analyses, we have discovered the catalytic active site and have identified Asp288 as the deprotonation residue and Lys290 as the autoacetylation residue. We have further proposed the unique H3-K56 anchoring pocket and the potential H3alphaN binding groove. Our work has provided structural insights to understand the acetylation mechanism of H3-K56 by Rtt109.

PubMed: 18707894
DOI: 10.1016/j.str.2008.07.006

実験手法

X-RAY DIFFRACTION (1.9 Å)