Structure of the WipA protein reveals a novel tyrosine protein phosphatase effector from <i>Legionella pneumophila</i>.

ABSTRACT: Legionnaires' disease is a severe form of pneumonia caused by the bacterium Legionella pneumophila. L. pneumophila pathogenicity relies on secretion of more than 300 effector proteins by a type IVb secretion system. Among these Legionella effectors, WipA has been primarily studied because of its dependence on a chaperone complex, IcmSW, for translocation through the secretion system, but its role in pathogenicity has remained unknown. In this study, we present the crystal structure of a large fragment of WipA, WipA435. Surprisingly, this structure revealed a serine/threonine phosphatase fold that unexpectedly targets tyrosine-phosphorylated peptides. The structure also revealed a sequence insertion that folds into an α-helical hairpin, the tip of which adopts a canonical coil

SUBMITTER: Pinotsis N 

PROVIDER: S-EPMC5454105 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature