5n72

Crystal structure of the Legionella effector WipA shorter construct

spinqualitylabelsall models 5n72, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n72 is a 1 chain structure with sequence from Legionella pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.842Å Ligands: ACT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5GA16_LEGPN Publication Abstract from PubMed 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 alpha-helical hairpin, the tip of which adopts a canonical coiled-coil structure. The purified protein was a dimer, whose dimer interface involves interactions between the coiled-coil of one WipA molecule and the phosphatase domain of another. Given the ubiquity of protein-protein interaction mediated by interactions between coiled-coils, we hypothesize that WipA can thereby transition from a homo-dimeric state to a hetero-dimeric state in which the coiled-coil region of WipA is engaged in a protein-protein interaction with a tyrosine-phosphorylated host target. In conclusion, these findings help advance our understanding of the molecular mechanisms of an effector involved in Legionella virulence and may inform approaches to elucidate the function of other effectors. Structure of the WipA protein reveals a novel tyrosine protein phosphatase effector from Legionella pneumophila.,Pinotsis N, Waksman G J Biol Chem. 2017 Apr 7. pii: jbc.M117.781948. doi: 10.1074/jbc.M117.781948. PMID:28389563 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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