ArticleNature communications2025
The mycobacterial ABC transporter IrtAB employs a membrane-facing crevice for siderophore-mediated iron uptake.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed.
- Advances in EPR Approaches for Studying Structural Properties of Membrane Proteins.Magnetic resonance in chemistry : MRC · 2026Review
- SOQS: Superposition of Quantum States for Selective Detection of Dipolar Frequency Multiples in Pulsed EPR Spectroscopy.ACS physical chemistry Au · 2026Article
- Review
- Studying the Protein-Membrane Interaction of a Mycobacterial ABC Transporter Through Coarse-Grained Simulations.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Review
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Authors and funding
8 authors.
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Abstract
The mycobacterial ABC transporter IrtAB features an ABC exporter fold, yet it imports iron-charged siderophores called mycobactins. Here, we present extensive cryo-EM analyses and DEER measurements, revealing that IrtAB alternates between an inward-facing and an outward-occluded conformation, but does not sample an outward-facing conformation. When IrtAB is locked in its outward-occluded conformation in nanodiscs, mycobactin is bound in the middle of the lipid bilayer at a membrane-facing crevice opening at the heterodimeric interface. Mutations introduced at the crevice abrogate mycobactin import and in corresponding structures, the crevice is collapsed. A conserved triple histidine motif coordinating a zinc ion is present below the mycobactin binding site. Substitution of these histidine residues with alanine results in a decoupled transporter, which hydrolyzes ATP, but lost its capacity to import mycobactins. Our data suggest that IrtAB imports mycobactin via a credit-card mechanism in a transport cycle that is coupled to the presence of zinc.
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