Extended Data Fig. 1: Interactions between MavL and Ub.
From: Legionella effector LnaB is a phosphoryl-AMPylase that impairs phosphosignalling
a, Native PAGE analyses of Ub, ADPRR42-Ub and PRR42-Ub after treatments by the cell lysates of the wild-type and sidE-deleted strains of L. pneumophila. b, In vitro ARH assays of MavL toward ADPRR42-Ub. The ADP-ribosyl hydrolysation of ADPRR42-Ub was examined by the mobility shifts on native PAGE gels and Coomassie blue staining. c, Interactions of MavL with polyUb and Ub. d, 2mFo-DFc and mFo-DFc electron density maps of Ub in the MavL–Ub complex. The 2mFo-DFc map is shown as blue meshes and contoured at 1.0 σ. The mFo-DFc map is shown as meshes coloured in green (positive) and red (negative) and contoured at 3.0 σ. e,f, Detailed interactions of MavL with Ub in the MavL–Ub complex structure. The mFo-DFc electron density map of the interacting residues (f) was calculated with the residues and loop regions removed and is shown as meshes coloured in green (positive) and red (negative) and contoured at 3.0 σ. g, Structural superimposition of MavL with Thermomonospora curvata PARG13 (PDB ID: 3SIG). The ADPR ligand in the PARG structure is represented as sticks in cyan. The catalytic pocket of MavL is highlighted within the dashed box. h, Close-up view of the ADPR-binding pockets of MavL and PARG. The catalytic residues of MavL and PARG are shown as sticks. i, Interactions of the catalytic pocket of MavL with the ADPR ligand that was modelled from PARG, according to the structural superimposition of MavL and PARG (g). j,k, Mutagenetic analyses of the Ub-interacting residues of MavL on its interactions with Ub (j) and its ARH activity (k). All uncropped and unprocessed scans of blots and gels are listed in Supplementary Fig. 1.
