EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 122, Issue 24, Page e2419096122, Year 2025
掲載日	2025年6月17日
著者	Jun Bae Park / Gwanwoo Lee / Yu-Yeon Han / Dongwook Kim / Kyoo Heo / Jeesoo Kim / Juhee Park / Hyosuk Yun / Chul Won Lee / Hyun-Soo Cho / Jong-Seo Kim / Martin Steinegger / Yeong-Jae Seok / Soung-Hun Roh /
PubMed 要旨	GCN5-related -acetyltransferases (GNATs) are essential for regulating bacterial metabolism by acetylating specific target proteins. Despite their importance in bacterial physiology, the mechanisms ...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.
リンク	Proc Natl Acad Sci U S A / PubMed:40498448 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	1.97 - 2.81 Å
構造データ	EMDB-60841: Consensus map of acetyltransferase 手法: EM (単粒子) / 解像度: 2.52 Å EMDB-60842: AGD-Focused map 手法: EM (単粒子) / 解像度: 2.47 Å EMDB-60843: GNATD focused acetyltransferase 手法: EM (単粒子) / 解像度: 2.43 Å EMDB-60844: RD of acetyltransferase 手法: EM (単粒子) / 解像度: 2.81 Å EMDB-60845: Consensus map of ligand bound acetyltransferase 手法: EM (単粒子) / 解像度: 1.99 Å EMDB-60846: AGD of acetyltransferase 手法: EM (単粒子) / 解像度: 1.97 Å EMDB-60847: GNATD of acetyltransferase 手法: EM (単粒子) / 解像度: 2.12 Å EMDB-60848: RD of acetyltransferase 手法: EM (単粒子) / 解像度: 1.99 Å 60849 9isq EMDB-60849, PDB-9isq: Apo-state E.coli PatZ 手法: EM (単粒子) / 解像度: 2.52 Å 60853 9it0 EMDB-60853, PDB-9it0: Liganded-state E.coli PatZ 手法: EM (単粒子) / 解像度: 1.99 Å PDB-9isb: Ligand bound AGD of enzyme 手法: X-RAY DIFFRACTION / 解像度: 2.24 Å
化合物	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP / ADP, エネルギー貯蔵分子YM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-HOH: WATER ChemComp-ACO: ACETYL COENZYME A / アデノシン3′-りん酸5′-[二りん酸P²-[(R)-3-ヒドロキシ-2,2-ジメチル-3-[[(以下略) ChemComp-PO4*: PHOSPHATE ION / ホスファ-ト
由来	escherichia coli bl21(de3) (大腸菌)
キーワード	TRANSFERASE / Acetyltransferase