8A9N

Structure of DpA polyamine acetyltransferase in complex with 1,3-DAP

8A9N の概要

• エントリーDOI: 10.2210/pdb8a9n/pdb
• 分子名称: Acetyltransferase, COENZYME A, MAGNESIUM ION, ... (7 entities in total)
• 機能のキーワード: polyamine acetyltransferase, gnat, bacterial biofilm formation, acinetorbacter baumannii, transferase
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38541.62

構造登録者

Garcia-Pino, A.,Jurenas, D. (登録日: 2022-06-28, 公開日: 2023-07-12, 最終更新日: 2024-02-07)

主引用文献

Armalyte, J.,Cepauskas, A.,Sakalyte, G.,Martinkus, J.,Skerniskyte, J.,Martens, C.,Suziedeliene, E.,Garcia-Pino, A.,Jurenas, D.
A polyamine acetyltransferase regulates the motility and biofilm formation of Acinetobacter baumannii.
Nat Commun, 14:3531-3531, 2023

PubMed Abstract: Acinetobacter baumannii is a nosocomial pathogen highly resistant to environmental changes and antimicrobial treatments. Regulation of cellular motility and biofilm formation is important for its virulence, although it is poorly described at the molecular level. It has been previously reported that Acinetobacter genus specifically produces a small positively charged metabolite, polyamine 1,3-diaminopropane, that has been associated with cell motility and virulence. Here we show that A. baumannii encodes novel acetyltransferase, Dpa, that acetylates 1,3-diaminopropane, directly affecting the bacterium motility. Expression of dpa increases in bacteria that form pellicle and adhere to eukaryotic cells as compared to planktonic bacterial cells, suggesting that cell motility is linked to the pool of non-modified 1,3-diaminopropane. Indeed, deletion of dpa hinders biofilm formation and increases twitching motion confirming the impact of balancing the levels of 1,3-diaminopropane on cell motility. The crystal structure of Dpa reveals topological and functional differences from other bacterial polyamine acetyltransferases, adopting a β-swapped quaternary arrangement similar to that of eukaryotic polyamine acetyltransferases with a central size exclusion channel that sieves through the cellular polyamine pool. The structure of catalytically impaired Dpa in complex with the reaction product shows that binding and orientation of the polyamine substrates are conserved between different polyamine-acetyltransferases.

PubMed: 37316480
DOI: 10.1038/s41467-023-39316-5

実験手法

X-RAY DIFFRACTION (1.854 Å)