5N72

Crystal structure of the Legionella effector WipA shorter construct

5N72 の概要

• エントリーDOI: 10.2210/pdb5n72/pdb
• 分子名称: WipA, ACETATE ION (3 entities in total)
• 機能のキーワード: legionella effector, tyrosine phosphatase, phosphoesterase fold, coiled-coil, hydrolase
• 由来する生物種: Legionella pneumophila
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 47434.92

構造登録者

Pinotsis, N.,Waksman, G. (登録日: 2017-02-17, 公開日: 2017-04-19, 最終更新日: 2024-05-08)

主引用文献

Pinotsis, N.,Waksman, G.
Structure of the WipA protein reveals a novel tyrosine protein phosphatase effector from Legionella pneumophila.
J. Biol. Chem., 292:9240-9251, 2017

PubMed Abstract: Legionnaires' disease is a severe form of pneumonia caused by the bacterium pathogenicity relies on secretion of more than 300 effector proteins by a type IVb secretion system. Among these 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 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 homodimeric state to a heterodimeric 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 virulence and may inform approaches to elucidate the function of other effectors.

PubMed: 28389563
DOI: 10.1074/jbc.M117.781948

実験手法

X-RAY DIFFRACTION (1.842 Å)