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. 2021 Oct 2;16(3):788–800. doi: 10.1038/s41396-021-01121-7

Fig. 6. Tertiary structure model of the sensory periplasmatic domain of the sensory histidine kinases PhoQ and CprS from Pseudomonas aeruginosa strain PAO1 (left panel) and Pseudomonas sp. MPFS (right panel), and modeled docking with the peptide raniseptin-Prs.

Fig. 6

A Both sensory domains form a PAS-like fold. B Net charge at pH = 7.0 and electrostatic potential (±2kT/e) visualized over molecular surface. The red to blue color gradient depicts the negative to positive potentials, respectively. The Asp and Glu residues near the expected membrane region are depicted for all sensory domains. C Structure of complexes of raniseptin-Prs with PhoQ and CprS and respective scores, in arbitrary energy units (a.e.u.), obtained by docking. The hydrophobic residues of raniseptin-Prs are shown as gray dots. Cytoplasmic membrane is represented only for reference.