5GCN

CATALYTIC DOMAIN OF TETRAHYMENA GCN5 HISTONE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A

5GCN の概要

• エントリーDOI: 10.2210/pdb5gcn/pdb
• 分子名称: HISTONE ACETYLTRANSFERASE GCN5, COENZYME A (2 entities in total)
• 機能のキーワード: histone acetyltransferase, chromatin remodeling, transcription regulation, transferase
• 由来する生物種: Tetrahymena thermophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20499.53

構造登録者

Lin, Y.,Fletcher, C.M.,Zhou, J.,Allis, C.D.,Wagner, G. (登録日: 1999-03-24, 公開日: 1999-07-19, 最終更新日: 2024-05-22)

主引用文献

Lin, Y.,Fletcher, C.M.,Zhou, J.,Allis, C.D.,Wagner, G.
Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A
Nature, 400:86-89, 1999

PubMed Abstract: Gene transcription requires the release of inactive DNA from its packaging of histone proteins. Following the discovery of the first transcription-associated histone acetyltransferase, tetrahymena GCN5, it was shown that yeast GCN5 is recruited to the promoter and causes hyper-acetylation of histones and transcriptional activation of target genes, establishing a direct connection between histone acetylation and transcriptional activation. Many other important transcription regulators have been found to have histone acetyltransferase activity, including TAFII230/250, p300/CBP and its associated factor PCAF. Here we present the solution structure of the catalytic domain of tGCN5 (residues 47-210) in complex with coenzyme A. The structure contains two domains; the amino-terminal domain is similar to those of other GCN5-related N-acetyltransferases but the carboxy-terminal domain is not. Coenzyme A binds in a deep hydrophobic pocket between the two domains. Chemical shift changes upon titration with histone H3 peptides indicate a binding site at the domain boundary opposite to the coenzyme A site. The structural data indicate a single-step acetyl-transfer reaction mechanism catalysed by a hydrogen bond to the backbone amide group of leucine 126 and the side-chain carboxyl group of a conserved acidic residue.

PubMed: 10403255
DOI: 10.1038/21922

実験手法

SOLUTION NMR