ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded state.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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Who cites it
102 citing papers in PubMed, 191 citations in OpenAlex.
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Decoding the Microcin J25 Biosynthetic Cluster: Modulation of theInternational journal of molecular sciences · 2026Article
- Review
- Structural insights into Arabidopsis thaliana CTS-mediated fatty acid and hormone metabolism.Nature communications · 2026Article
- Cryo-EM of human P-glycoprotein reveals an intermediate occluded conformation during active drug transport.Nature communications · 2025Article
- The mycobacterial ABC transporter IrtAB employs a membrane-facing crevice for siderophore-mediated iron uptake.Nature communications · 2025Article
- Nucleotide asymmetry and flexible linker dynamics modulate drug efflux cycle of P-glycoprotein, A computational study.Computational and structural biotechnology journal · 2025Article
- Outsmarting Nightmare: Drug Resistance inThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2025Review
- Inside-out, antimicrobial resistance mediated by efflux pumps in clinical strains of Acinetobacter baumannii isolated from burn wound infections.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Structural basis of prostaglandin efflux by MRP4.Nature structural & molecular biology · 2024Article
- Asymmetric conformations and lipid interactions shape the ATP-coupled cycle of a heterodimeric ABC transporter.Nature communications · 2023Article
- Structural basis of peptide secretion for Quorum sensing by ComA.Nature communications · 2023Article
- Experimental phasing opportunities for macromolecular crystallography at very long wavelengths.Communications chemistry · 2023Article
- Antimicrobial Resistance: Two-Component Regulatory Systems and Multidrug Efflux Pumps.Antibiotics (Basel, Switzerland) · 2023Review
- ABC Transporters in Bacterial Nanomachineries.International journal of molecular sciences · 2023Review
- The culmination of multidrug-resistant efflux pumps vs. meager antibiotic arsenal era: Urgent need for an improved new generation of EPIs.Frontiers in microbiology · 2023Review
- Review
- The ABC transporter MsbA adopts the wide inward-open conformation inScience advances · 2022Article
- Functionalization of Se-Te Nanorods with Au Nanoparticles for Enhanced Anti-Bacterial and Anti-Cancer Activities.Materials (Basel, Switzerland) · 2022Article
- Asymmetric drug binding in an ATP-loaded inward-facing state of an ABC transporter.Nature chemical biology · 2022Article
42 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
Enterobacteriaceae produce antimicrobial peptides for survival under nutrient starvation. Microcin J25 (MccJ25) is an antimicrobial peptide with a unique lasso topology. It is secreted by the ATP-binding cassette (ABC) exporter McjD, which ensures self-immunity of the producing strain through efficient export of the toxic mature peptide from the cell. Here we have determined the crystal structure of McjD from Escherichia coli at 2.7-Å resolution, which is to the authors' knowledge the first structure of an antibacterial peptide ABC transporter. Our functional and biochemical analyses demonstrate McjD-dependent immunity to MccJ25 through efflux of the peptide. McjD can directly bind MccJ25 and displays a basal ATPase activity that is stimulated by MccJ25 in both detergent solution and proteoliposomes. McjD adopts a new conformation, termed nucleotide-bound outward occluded. The new conformation defines a clear cavity; mutagenesis and ligand binding studies of the cavity have identified Phe86, Asn134, and Asn302 as important for recognition of MccJ25. Comparisons with the inward-open MsbA and outward-open Sav1866 structures show that McjD has structural similarities with both states without the intertwining of transmembrane (TM) helices. The occluded state is formed by rotation of TMs 1 and 2 toward the equivalent TMs of the opposite monomer, unlike Sav1866 where they intertwine with TMs 3-6 of the opposite monomer. Cysteine cross-linking studies on the McjD dimer in inside-out membrane vesicles of E. coli confirmed the presence of the occluded state. We therefore propose that the outward-occluded state represents a transition intermediate between the outward-open and inward-open conformation of ABC exporters.
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