Fig. 8: Model for DosP allostery.
a Schematic of DosP derived from the atomic model for DosPFLAG-WT bound to c-di-GMP. The two DosP monomers and domains are labeled. Sites interrogated through mutagenesis are highlighted with brackets. Mutations colored red reduce the catalytic activity of DosP, and mutations colored blue increase the catalytic activity of DosP. b Model for DosP allostery. In the absence of substrate, DosP exists in two conformations. Substrate binding stabilizes an oxy-state ON or deoxy-state OFF form. c Schematic for the state of the EAL domain in the oxy and deoxy-states without and with substrate.
