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-Structure paper
タイトル | Structure, Function, and Evolution of the Pseudomonas aeruginosa Lysine Decarboxylase LdcA. |
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ジャーナル・号・ページ | Structure, Vol. 27, Issue 12, Page 1842-11854.e4, Year 2019 |
掲載日 | 2019年12月3日 |
![]() | Eaazhisai Kandiah / Diego Carriel / Pierre Simon Garcia / Jan Felix / Manuel Banzhaf / George Kritikos / Maria Bacia-Verloop / Céline Brochier-Armanet / Sylvie Elsen / Irina Gutsche / ![]() ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.7 Å |
構造データ | |
化合物 | ![]() ChemComp-PLP: |
由来 |
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![]() | OXIDOREDUCTASE / bacterial stress response |