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. Author manuscript; available in PMC: 2023 Dec 1.
Published in final edited form as: Structure. 2022 Nov 14;30(12):1626–1636.e4. doi: 10.1016/j.str.2022.10.008

Figure 1. Structure and function of the RhlR-PqsE complex in P. aeruginosa.

Figure 1.

a) Schematic of the domain architecture of RhlR and PqsE, with variants from the current study displayed in white boxes, in addition to previously characterized mutations displayed in green boxes for RhlR and purple boxes for PqsE. LBD = ligand binding domain, DBD = DNA binding domain, MBL = metallo-beta-lactamase domain. b) Schematic representation of the different mechanisms of RhlR (green) activation by C4HSL (orange) and/or PqsE (purple). c) SDS-PAGE gel depicting the purified fractions from Superdex-200 size exclusion chromatography. d) Structure of RhlR (green) bound to PqsE (purple) (top) or RhlR (green) bound to PqsE (purple) bound to DNA (bottom). e) Close-up view of the cross-domain conformation of the RhlR DBD domains. Residues F53, R55, and N76 in the RhlR LBD are highlighted. f) Close-up view of the cross-domain conformation of the RhlR DBD domains bound to DNA. Residues K217 and K228 in the RhlR DBD are highlighted. All structure images were created using Pymol. See also Figures S1–3.