Figure 5
Comparison of the primary and the predicted secondary and quaternary structures of the paralogous response regulators ApsR and PsdR from L. paracasei BL23. (A) The secondary structure of ApsR and PsdR receiver domains (RD) and DNA binding domains (DBD) based on predictions by Swiss Model30 is displayed as α-helices (black boxes) and β-sheets (grey boxes). Amino acids positions are indicated on top of the sequences. Conserved amino acids between both response regulators primary sequences are indicated in red under the secondary structures. (B) Ribbon representation of overlaying quaternary structures of ApsR (pink) and PsdR (green) based on predictions by Swiss Model30 showing the conservation of their predicted structural organizations. The RRs are displayed as asymmetric homodimers in an active-like conformation (see Materials and methods for further detail on the crystal structures used as templates for homology modeling). The positions of the receiver domains (RD) and the DNA binding domains (DBD) from each monomer are indicated.
