Journal
STRUCTURE
Volume 27, Issue 12, Pages 1842-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2019.10.003
Keywords
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Funding
- European Union [647784]
- GRAL [ANR-10-LABX-49-01]
- FRISBI within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-INSB-05-02]
- GRAL within the Grenoble Partnership for Structural Biology (PSB) [ANR-10-LABX-49-01]
- Rhone-Alpes Region
- Fondation pour la Recherche Medicale (FRM)
- fonds FEDER
- Centre National de la Recherche Scientifique (CNRS)
- Commissariat a l'Energie Atomique et aux Energies Alternatives (CEA)
- Universite Grenoble Alpes (UGA), EMBL
- GIS-Infrastructures en Biologie Sante et Agronomie (IBISA)
- LABEX GRAL
- ARC1 Sante Rhone-Alpes Auvergne
- long-term EMBO fellowship [ALTF441-2017]
- [ANR-16-CE02-0005]
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The only enzyme responsible for cadaverine production in the major multidrug-resistant human pathogen Pseudomonas aeruginosa is the lysine decarboxylase LdcA. This enzyme modulates the general polyamine homeostasis, promotes growth, and reduces bacterial persistence during carbenicillin treatment. Here we present a 3.7-angstrom resolution cryoelectron microscopy structure of LdcA. We introduce an original approach correlating phylogenetic signal with structural information and reveal possible recombination among LdcA and arginine decarboxylase subfamilies within structural domain boundaries. We show that LdcA is involved in full virulence in an insect pathogenesis model. Furthermore, unlike its enterobacterial counterparts, LdcA is regulated neither by the stringent response alarmone ppGpp nor by the AAA+ ATPase RavA. Instead, the P. aeruginosa ravA gene seems to play a defensive role. Altogether, our study identifies LdcA as an important player in P. aeruginosa physiology and virulence and as a potential drug target.
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