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TitleStructure, Function, and Evolution of the Pseudomonas aeruginosa Lysine Decarboxylase LdcA.
Journal, issue, pagesStructure, Vol. 27, Issue 12, Page 1842-11854.e4, Year 2019
Publish dateDec 3, 2019
AuthorsEaazhisai Kandiah / Diego Carriel / Pierre Simon Garcia / Jan Felix / Manuel Banzhaf / George Kritikos / Maria Bacia-Verloop / Céline Brochier-Armanet / Sylvie Elsen / Irina Gutsche /
PubMed AbstractThe 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 ...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-Å 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.
External linksStructure / PubMed:31653338
MethodsEM (single particle)
Resolution3.7 Å
Structure data

4468

6q6i

EMDB-4468, PDB-6q6i:
Lysine decarboxylase A from Pseudomonas aeruginosa
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

Source
  • pseudomonas aeruginosa (bacteria)
KeywordsOXIDOREDUCTASE / bacterial stress response

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