9IT0

Liganded-state E.coli PatZ

9IT0 の概要

• エントリーDOI: 10.2210/pdb9it0/pdb
• EMDBエントリー: 60853
• 分子名称: Protein acetyltransferase, ACETYL COENZYME *A, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: acetyltransferase, transferase
• 由来する生物種: Escherichia coli BL21(DE3)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 399253.95

構造登録者

Park, J.B.,Roh, S.H. (登録日: 2024-07-19, 公開日: 2025-06-04, 最終更新日: 2025-06-25)

主引用文献

Park, J.B.,Lee, G.,Han, Y.Y.,Kim, D.,Heo, K.,Kim, J.,Park, J.,Yun, H.,Lee, C.W.,Cho, H.S.,Kim, J.S.,Steinegger, M.,Seok, Y.J.,Roh, S.H.
Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.
Proc.Natl.Acad.Sci.USA, 122:e2419096122-e2419096122, 2025

PubMed Abstract: GCN5-related -acetyltransferases (GNATs) are essential for regulating bacterial metabolism by acetylating specific target proteins. Despite their importance in bacterial physiology, the mechanisms behind their enzymatic and regulatory functions remain poorly understood. In this study, we investigated the structures of protein acetyltransferase Z (PatZ), a Type I GNAT, and examined its ligand interactions, catalytic mechanism, and allosteric regulation. PatZ functions as a homotetramer, with each subunit comprising a catalytic and a regulatory domain. Our results demonstrate that the regulatory domain is vital for acetyltransferase activity, as it triggers cooperative conformational changes in the catalytic domain and directly aids in the formation of substrate-binding pockets. Additionally, a protein structure-based evolutionary analysis of bacterial GNAT types revealed a distinct regulatory domain pattern across phyla, highlighting its crucial role in responding to cellular energy levels.

PubMed: 40498448
DOI: 10.1073/pnas.2419096122

実験手法

ELECTRON MICROSCOPY (1.99 Å)