Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ

GCN5-related <i>N</i>-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 <i>Escherichia coli</i> 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.

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Journal
Proceedings of the National Academy of Sciences
Published
2025-06-11
DOI
https://doi.org/10.1073/pnas.2419096122
Primary Topic
Enzyme Structure and Function
Type
article
Field-Weighted Citation Impact
0.00

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article

Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ

Hyosuk Yun, Martin Steinegger, Jun Bae Park, Chul Won Lee et al.
Proceedings of the National Academy of Sciences
Enzyme Structure and Function
article

Structural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ

Hyosuk Yun, Martin Steinegger, Jun Bae Park, Chul Won Lee, Jeesoo Kim, Yeong‐Jae Seok, Kyoo Heo, Yu-Yeon Han, Soung‐Hun Roh, Gwanwoo Lee, Jong‐Seo Kim, Dongwook Kim, Ju-Hee Park, Hyun‐Soo Cho
article en

Abstract

GCN5-related <i>N</i>-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 <i>Escherichia coli</i> 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.

Proceedings of the National Academy of SciencesVol. 122(24)
Chonnam National University (KR), Seoul National University (KR), Yonsei University (KR), Institute for Basic Science (KR), Czech Academy of Sciences, Institute of Microbiology (CZ), Institute of Molecular Biology and Genetics (UA)
National Research Foundation of Korea
Openalex Percentile: Top 91%
Enzyme Structure and Function
DOIOpen Access PDFOpenAlex
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