Fig. 3: Confirmation of the NC-RBS complex interface.
From: Rab1-AMPylation by Legionella DrrA is allosterically activated by Rab1
a Melting point (Tm) determination of DrrA and DrrA alanine mutants by circular dichroism (CD). The melting point of wt DrrA is 60.1 °C. Data are means ± standard error of the mean (SEM) from three independent experiments. b Determination of Rab1b-AMPylation rates in vitro by DrrA with mutations in the non-conventional site. The kcat/KM value of wt DrrA is 8.0 × 105 M−1 s−1 (± 2.0 × 104 M−1 s−1). Data are means ± standard error of the mean (SEM) from three independent experiments. c Representation of selected interactions for in cellulo crosslinking in E. coli. Pink spheres are the catalytic Asp residues of DrrA. d Pairwise BrC6K (within Rab1b) and Cys mutations (within DrrA) based on the DrrA:TReND-1:Rab complex lead to covalent crosslink formation, if the BrC6K-based thioether linker is able to bridge the Rab1b-DrrA interface, as observed by α-His6 and α-Strep western-blotting. Source data are provided as a Source Data file.
