Crystal structure of the Legionella pneumophila FIC domain-containing effector AnkX protein (inactive H229A mutant) in complex with cytidine-diphosphate-choline
This entry represents the insertion domain of AnkX, a Legionella pneumophila PC transferase that mediates the recruitment of Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). It is a virulence factor that modifies host RAB1 (RAB ...
This entry represents the insertion domain of AnkX, a Legionella pneumophila PC transferase that mediates the recruitment of Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). It is a virulence factor that modifies host RAB1 (RAB1A, RAB1B, or RAB1C) and RAB35 leading to the displacement of GDP dissociation inhibitors (GDI) and impairs accessibility to the GTPase effector LepB. It consists of two distinct structural units. The N-terminal contains a FIC domain, which encompasses the CDP-choline binding pocket and a C-terminal ankyrin repeats-containing domain [1,2]. Unlike other FIC enzymes, AnkX comprises an additional insert domain located in the conserved beta-hairpin which consists of alpha-helices and beta-sheets that protrudes from the enzyme and adapts a rigid, thorn-like structure [2].