Fig. 4: Structural details of DosP^WT with bound c-di-GMP.

a Composite map of DosP^FLAG-WT with the bound c-di-GMP from three orientations. Density for the two chains are shown as cyan and yellow density maps at a contour level of 0.064. The density for c-di-GMP and heme is shown in magenta and red, respectively. The density of magnesium is shown in green. Axial dimensions are labeled. b Atomic model depicted as cartoon and overlaid with a map that was gaussian filtered to level 1.5. Domains of DosP are labeled. c close view of a single EAL domain with bound c-di-GMP. Density for the EAL domain is colored cyan, c-di-GMP density is colored magenta, and magnesium density is colored green. d Density for c-di-GMP shown in two orientations. The c-di-GMP is represented as sticks and the density map displayed as a blue mesh carved at 2.0 Å and sigma=10. e DosP^FLAG-WT and DosP^R97A residues 639-662 superposed and displayed with blue and purple cartoon, respectively. L647 is depicted with yellow spheres and c-di-GMP is depicted in sticks. Arrow indicates the change in position of L647 between the two forms of DosP. Panels a-c generated using ChimeraX. Panels d-e generated using PyMOL. hPAS, heme-binding Per-Arnt-Sim; EAL, c-di-GMP phosphodiesterase domain; EGTQF- diguanylate cyclase domain.