8A9O
Structure of the polyamine acetyltransferase DpA
Summary for 8A9O
| Entry DOI | 10.2210/pdb8a9o/pdb |
| Descriptor | DpA polyamine acetyltransferase, COENZYME A, BROMIDE ION, ... (7 entities in total) |
| Functional Keywords | polyamine acetyltransferase, gnat, bacterial biofilm formation, acinetorbacter baumannii, transferase |
| Biological source | Acinetobacter baumannii |
| Total number of polymer chains | 2 |
| Total formula weight | 39817.53 |
| Authors | Garcia-Pino, A.,Jurenas, D. (deposition date: 2022-06-28, release date: 2023-07-12, Last modification date: 2023-11-22) |
| Primary citation | 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 Cited by 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: 37316480DOI: 10.1038/s41467-023-39316-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.587 Å) |
Structure validation
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