5FYA

Cubic crystal of the native PlpD

Summary for 5FYA

• Entry DOI: 10.2210/pdb5fya/pdb
• Descriptor: PATATIN-LIKE PROTEIN, PLPD (2 entities in total)
• Functional Keywords: hydrolase, bacterial secretion, phospholipase, lipid affinity, infection
• Biological source: PSEUDOMONAS AERUGINOSA
• Total number of polymer chains: 2
• Total formula weight: 67825.90

Authors

Vinicius da Mata Madeira, P.,Zouhir, S.,Basso, P.,Neves, D.,Laubier, A.,Salacha, R.,Bleves, S.,Faudry, E.,Contreras-Martel, C.,Dessen, A. (deposition date: 2016-03-04, release date: 2016-04-06, Last modification date: 2024-01-10)

Primary citation

Da Mata Madeira, P.V.,Zouhir, S.,Basso, P.,Neves, D.,Laubier, A.,Salacha, R.,Bleves, S.,Faudry, E.,Contreras-Martel, C.,Dessen, A.
Structural Basis of Lipid Targeting and Destruction by the Type V Secretion System of Pseudomonas Aeruginosa.
J.Mol.Biol., 428:1790-, 2016

PubMed 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.

PubMed: 27012424
DOI: 10.1016/J.JMB.2016.03.012

Experimental method

X-RAY DIFFRACTION (2.141 Å)