The Binding of Triclosan to SmeT, the Repressor of the Multidrug Efflux Pump SmeDEF, Induces Antibiotic Resistance in Stenotrophomonas maltophilia
Figure 7
Structural details of the triclosan binding site.
(A) The Fo-Fc omit electron density map contoured at 2.4 σ around the triclosan molecules is shown in red. (B) Key interactions (H-bonds in orange) between the triclosan molecules and the binding pocket residues of SmeT (distances less than 4 Å). The most important residues in the formation of the binding pocket are shown and labeled. (C) The binding of two molecules of triclosan displaces residues His-167, Leu-114 and Met-113. These last two residues belong to helix a6, which interacts trough H bonds with helix a1, part of the DNA binding domain of SmeT.