Fig. 1: Structure of Hoechst-bound BmrCD in an outward-facing conformation. | Nature Communications

Fig. 1: Structure of Hoechst-bound BmrCD in an outward-facing conformation.

From: Drug-bound outward-facing conformation of a heterodimeric ABC exporter suggests a putative mechanism of drug translocation

Fig. 1

a Cryo-EM map and structure model of BmrCD OF conformation bound to Hoechst. The extracellular domain (ECD), transmembrane domain (TMD), and nucleotide-binding domain (NBD) are indicated. BmrC and BmrD are shown in light sea green and tan. Hoechst (HT) and ATP/ADPVi are shown as sticks in magenta, and lipids are blue, hereafter if not indicated. b Conformational changes of the TMD intracellular (left panels) and extracellular sides (right panels) between BmrCD_OF, BmrCD_IF (PDB 8FMV), and BmrCD_OC (PDB 8T1P). All alignments are based on BmrD. BmrCD_IF and BmrCD_OC are shown in gray and slate, respectively. Large movements are indicated by red arrows. c DEER distance distributions for spin-label pairs on the intracellular (96BmrC/188BmrD) and extracellular (55BmrC/146BmrD) sides in BmrCD. Upper panels: close-up views of BmrCD_OF highlighting spin label pairs. TMD helices are shown as cylinders, ECD and NBD are shown as transparent surfaces. The spin-labeled locations are shown by raspberry spheres. Lower panels: experimental distance distributions are shown in solid lines. Simulate distance distributions derived from cryo-EM structures by MDDS are shown in dashed lines.

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