Structural highlights
Publication Abstract from PubMedThe 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 beta-barrel. Here we report the crystal structure of the secreted form of PlpD in its biologically active state. PlpD displays a classical lipase alpha/beta 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. Structural Basis of Lipid Targeting and Destruction by the Type V Secretion System of Pseudomonas aeruginosa.,da Mata Madeira PV, Zouhir S, Basso P, Neves D, Laubier A, Salacha R, Bleves S, Faudry E, Contreras-Martel C, Dessen A J Mol Biol. 2016 May 8;428(9 Pt A):1790-803. doi: 10.1016/j.jmb.2016.03.012. Epub, 2016 Mar 21. PMID:27012424[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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