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Structural Basis of Lipid Targeting and Destruction by the Type V Secretion System of Pseudomonas aeruginosa.

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.
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Contributeur : Frank Thomas <>
Soumis le : jeudi 7 juillet 2016 - 11:39:58
Dernière modification le : mercredi 7 octobre 2020 - 03:15:03




Paulo Vinicius da Mata Madeira, Samira Zouhir, Pauline Basso, David Neves, Aurélie Laubier, et al.. Structural Basis of Lipid Targeting and Destruction by the Type V Secretion System of Pseudomonas aeruginosa.. Journal of Molecular Biology, Elsevier, 2016, 428 (9 Pt A), pp.1790-803. ⟨10.1016/j.jmb.2016.03.012⟩. ⟨hal-01342981⟩



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