1. Structural Basis of Lipid Targeting and Destruction by the Type V Secretion System of Pseudomonas aeruginosa.
- Author
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da Mata Madeira PV, Zouhir S, Basso P, Neves D, Laubier A, Salacha R, Bleves S, Faudry E, Contreras-Martel C, and Dessen A
- Subjects
- Catalytic Domain, Crystallography, X-Ray, Models, Molecular, Phosphatidylinositols metabolism, Protein Conformation, Substrate Specificity, Type V Secretion Systems metabolism, Bacterial Proteins chemistry, Bacterial Proteins metabolism, Phospholipases chemistry, Phospholipases metabolism, Pseudomonas aeruginosa enzymology
- Abstract
The type V secretion system is a macromolecular machine employed by a number of bacteria to secrete virulence factors into the environment. The human pathogen Pseudomonas aeruginosa employs the newly described type Vd secretion system to secrete a soluble variant of PlpD, a lipase of the patatin-like family synthesized as a single macromolecule that also carries a polypeptide transport-associated domain and a 16-stranded β-barrel. Here we report the crystal structure of the secreted form of PlpD in its biologically active state. PlpD displays a classical lipase α/β hydrolase fold with a catalytic site located within a highly hydrophobic channel that entraps a lipidic molecule. The active site is covered by a flexible lid, as in other lipases, indicating that this region in PlpD must modify its conformation in order for catalysis at the water-lipid interface to occur. PlpD displays phospholipase A1 activity and is able to recognize a number of phosphatidylinositols and other phosphatidyl analogs. PlpD is the first example of an active phospholipase secreted through the type V secretion system, for which there are more than 200 homologs, revealing details of the lipid destruction arsenal expressed by P. aeruginosa in order to establish infection., (Copyright © 2016 Elsevier Ltd. All rights reserved.)
- Published
- 2016
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