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

• 成果类型: Article
• 署名作者: Park, Jun Bae; Lee, Gwanwoo; Han, Yu - Yeon; Kim, Dongwook; Heo, Kyoo; Kim, Jeesoo; Park, Juhee; Yun, Hyosuk; Lee, Chul Won; Cho, Hyun- Soo; Kim, Jong- Seo; Steinegger, Martin; Seok, Yeong- Jae; Roh, Soung- Hun
• 署名单位: Seoul National University (SNU); Seoul National University (SNU); Seoul National University (SNU); Seoul National University (SNU); Seoul National University (SNU); Institute for Basic Science - Korea (IBS); Chonnam National University; Yonsei University
• 刊物名称: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
• ISSN/ISSBN: 0027-15014
• DOI: 10.1073/pnas.2419096122
• 发表日期: 2025-06-11
• 关键词: acetyl-coa synthetase; gcn5-related n-acetyltransferases; protein acetyltransferase; lysine acetylation; escherichia-coli; histone acetylation; crystal-structure; molecular-basis; metabolism; transcription

摘要

GCN5- related N- 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 Escherichia coli protein alytic 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 of bacterial GNAT types revealed a distinct regulatory domain pattern across phyla, highlighting its crucial role in responding to cellular energy levels.