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Structure paper

TitleStructural basis of the catalytic and allosteric mechanism of bacterial acetyltransferase PatZ.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 122, Issue 24, Page e2419096122, Year 2025
Publish dateJun 17, 2025
AuthorsJun 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 AbstractGCN5-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.
External linksProc Natl Acad Sci U S A / PubMed:40498448 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.97 - 2.81 Å
Structure data

EMDB-60841: Consensus map of acetyltransferase
Method: EM (single particle) / Resolution: 2.52 Å

EMDB-60842: AGD-Focused map
Method: EM (single particle) / Resolution: 2.47 Å

EMDB-60843: GNATD focused acetyltransferase
Method: EM (single particle) / Resolution: 2.43 Å

EMDB-60844: RD of acetyltransferase
Method: EM (single particle) / Resolution: 2.81 Å

EMDB-60845: Consensus map of ligand bound acetyltransferase
Method: EM (single particle) / Resolution: 1.99 Å

EMDB-60846: AGD of acetyltransferase
Method: EM (single particle) / Resolution: 1.97 Å

EMDB-60847: GNATD of acetyltransferase
Method: EM (single particle) / Resolution: 2.12 Å

EMDB-60848: RD of acetyltransferase
Method: EM (single particle) / Resolution: 1.99 Å

60849

9isq

EMDB-60849, PDB-9isq:
Apo-state E.coli PatZ
Method: EM (single particle) / Resolution: 2.52 Å

60853

9it0

EMDB-60853, PDB-9it0:
Liganded-state E.coli PatZ
Method: EM (single particle) / Resolution: 1.99 Å

PDB-9isb:
Ligand bound AGD of enzyme
Method: X-RAY DIFFRACTION / Resolution: 2.24 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

ChemComp-ACO:
ACETYL COENZYME *A

ChemComp-PO4:
PHOSPHATE ION

Source
  • escherichia coli bl21(de3) (bacteria)
KeywordsTRANSFERASE / Acetyltransferase

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