Fig. 5: The DosP catalytic pocket.

a Bound c-di-GMP is shown as blue sticks. The guanine bases are labeled G1 and G2. The two magnesium ions are shown as green spheres and labeled Me1 and Me2. Metal-coordinating residues are depicted as cyan sticks. The rest of the EAL domain is depicted as a transparent cartoon. b Residues interacting with c-di-GMP are shown as magenta sticks. The rest of the EAL domain is depicted as transparent cartoon. c Bar graph showing the kcat values determined from the turnover of 2 µM c-di-GMP at 25 °C by 10 nM aerobic DosPWT, DosPE584A, DosPR588A, DosPR588E, and DosPY784A. Value for DosPWT was taken from Fig. 1g, values for mutants are the mean of two independent experiments. The buffer for the assays was 20 mM Tris-HCl, 2.5 mM MgCl2, 2.0 mM DTT, pH 8.0. Residues whose substitutions were tested in c are highlighted with circles in a and b. Panels a and b generated with PyMOL. Source data are provided as a Source Data file.