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J Mol Biol. 2016 May 8;428(9 Pt A):1790-803. doi: 10.1016/j.jmb.2016.03.012. Epub 2016 Mar 21.

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

Author information

1
Brazilian National Laboratory for Biosciences (LNBio), CNPEM, Campinas, São Paulo, Brazil.
2
Univ. Grenoble Alpes, Bacterial Pathogenesis and Cellular Responses Group, Institut de Biosciences et Biotechnologies de Grenoble (BIG), Grenoble, France; CNRS, IBS and BIG, Grenoble, France; CEA, IBS and BIG, Grenoble, France; INSERM, UMR-S 1036 Biology of Cancer and Infection Laboratory, Grenoble, France.
3
CNRS & Aix-Marseille Université, Laboratoire d'Ingénierie des Systèmes Macromoléculaires (UMR7255), Institut de Microbiologie de la Méditerranée, Marseille, France.
4
CNRS, IBS and BIG, Grenoble, France; CEA, IBS and BIG, Grenoble, France; Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), Grenoble, France. Electronic address: carlos.contreras@ibs.fr.
5
Brazilian National Laboratory for Biosciences (LNBio), CNPEM, Campinas, São Paulo, Brazil; CNRS, IBS and BIG, Grenoble, France; CEA, IBS and BIG, Grenoble, France; Univ. Grenoble Alpes, Institut de Biologie Structurale (IBS), Grenoble, France. Electronic address: andrea.dessen@ibs.fr.

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.

KEYWORDS:

bacterial secretion; crystallography; infection; lipid affinity; phospholipase

PMID:
27012424
DOI:
10.1016/j.jmb.2016.03.012
[Indexed for MEDLINE]

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