Fig. 4: PstSCAB structure in the outward-facing, catalytic intermediate state.
From: Molecular mechanism of phosphate import by the bacterial PstSCAB transporter
a, b Cryo-EM density map (a) and cartoon representation (b) of PstSCAB structure in the outward-facing, catalytic intermediate state. c Binding of ATP at the interface between two PstBs. Interactions of the N-lobe of PstS with PstA (d), and the C-lobe of PstS with PstC (e). Hydrogen bonds are shown as green dashed lines. f Pi binding site in the TMD, with modeled Pi shown as sticks, and its density shown as mesh (contoured at rmsd threshold of 3 Å). g Distance distribution histograms between the Pi molecule and the proximal residues from all MD runs. The distances were measured as the minimum distance between any atom pairs of two residue groups, including side chains. h Binding curves for Pi with purified PstCAB and its Pi-coordinating residue mutants, measured with MST assays. i Pi import activity of Pi binding residue mutants. In g data represent mean ± SD (for all data points in each run, n = 2000). In data represent mean ± SD (biological replicates, n = 3 for h, n = 3 for i), except for the control (biological replicates, n = 2) and PstCE241QAB (biological replicates, n = 4) in (h). Source data are provided as a Source data file.
