1MJ9

Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A

1MJ9 の概要

• エントリーDOI: 10.2210/pdb1mj9/pdb
• 関連するPDBエントリー: 1FY7 1MJA 1MJB
• 分子名称: ESA1 PROTEIN, SODIUM ION, COENZYME A, ... (4 entities in total)
• 機能のキーワード: esa1, hat, histone acetyltransferase, myst, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34146.88

構造登録者

Yan, Y.,Harper, S.,Speicher, D.,Marmorstein, R. (登録日: 2002-08-27, 公開日: 2002-10-30, 最終更新日: 2024-02-14)

主引用文献

Yan, Y.,Harper, S.,Speicher, D.W.,Marmorstein, R.
The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate.
Nat.Struct.Biol., 9:862-869, 2002

PubMed Abstract: Yeast ESA1 is a member of the MYST subfamily of histone acetyltransferases (HATs), which use acetyl-coenzyme A (CoA) to acetylate specific Lys residues within histones to regulate gene expression. The structure of an ESA1-CoA complex reveals structural similarity to the catalytic core of the GCN5/PCAF subfamily of HAT proteins. Here we report additional structural and functional studies on ESA1 that demonstrate that histone acetylation proceeds through an acetyl-cysteine enzyme intermediate. This Cys residue is strictly conserved within the MYST members, suggesting a common mode of catalysis by this HAT subfamily. However, this mode of catalysis differs dramatically from the GCN5/PCAF subfamily, which mediate direct nucleophilic attack of the acetyl-CoA cofactor by the enzyme-deprotonated substrate lysine of the histone. These results demonstrate that different HAT subfamilies can use distinct catalytic mechanisms, which have implications for their distinct biological roles and for the development of HAT-specific inhibitors.

PubMed: 12368900
DOI: 10.1038/nsb0902-638

実験手法

X-RAY DIFFRACTION (2.5 Å)