Fig. 2: The AauA solute binding protein of EHEC displays higher affinity for D-ribulose over L-arabinose.
From: Convergent evolution of distinct D-ribulose utilisation pathways in attaching and effacing pathogens
a, NanoDSF data depicting the shift in melting temperature (∆Tm) of purified AauA in the presence of decreasing concentrations (2-fold dilutions from 7.5 mM to 0.03 mM (Right to left)) of ʟ-arabinose (green) or D-ribulose (blue). The buffer only control is illustrated in bold. NanoDSF melting experiments were performed in technical triplicate (n = 3). b, Representative ITC thermogram of ʟ-arabinose titrated into purified AauA. The integration of heats derivative curve is illustrated on the right, with the corresponding calculated Kd shown. c Equivalent ITC data quantifying the binding of AauA with D-ribulose. d X-ray crystal structure (Green) of AauA bound with D-ribulose (Blue) at the binding cleft. The N- and C-termini are indicated. e Detailed view of the binding cleft and the interactions formed between the residues of AauA with D-ribulose shown as sticks. Hydrogen bonds are represented as black dashed lines. Source data are provided as a Source Data file.
