Fig. 2: Structure of IrtAB in complex with mycobactin. | Nature Communications

Fig. 2: Structure of IrtAB in complex with mycobactin.

From: The mycobacterial ABC transporter IrtAB employs a membrane-facing crevice for siderophore-mediated iron uptake

Fig. 2

a Cryo-EM structures of inward-facing IrtAB (left panel, Dataset #1, PDB 9FXC) and outward-occluded 2xEQ-IrtAB (right panel, Dataset #5, PDB 9FW3), both obtained in nanodiscs. Shown are the surface representations of the modeled structures. IrtA is colored teal, IrtB magenta, and bound Fe-MBT in orange sticks. The membrane boundaries are indicated in gray planes. b Cryo-EM map of outward-occluded 2xEQ-IrtAB (Dataset #5, PDB 9FW3) with non-proteinaceous densities contoured at 5 σ and colored in orange (accounted for Fe-MBT) or in gray (likely stemming from lipids and the nanodiscs belt protein). c Detailed depiction of Fe-MBT binding site at the membrane-facing crevice formed between TMH2IrtA and TMH5IrtB. Side chains interacting with Fe-MBT are highlighted as sticks.

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