ArticleCommunications biology2025
In situ structure and assembly of the ABC-type tripartite pump MacAB-TolC.
Article in Communications biology, 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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Who cites it
5 citing papers in PubMed.
- Effect of polymyxin resistance evolution on the fitness costs of Acinetobacter baumannii and the underlying mechanisms of polymyxin resistance.Scientific reports · 2026Article
- Antibacterial Mechanism of Dipicolinic Acid AgainstBiomolecules · 2026Article
- Beyond Ribosomal Mutations: Identification ofMicroorganisms · 2026Article
- A review of research progress on periplasmic adaptor proteins in bacterial tripartite pumps.Frontiers in microbiology · 2026Review
- MarA binds and activates the ABC efflux pump YadGH to confer conditional macrolide resistance in AcrB-deficientFrontiers in microbiology · 2026Article
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Authors and funding
10 authors.
Funding
Abstract
The MacAB-TolC tripartite efflux pump is widely distributed in Gram-negative bacteria, extruding antibiotics and virulence factors that lead to multidrug resistance and pathogenicity. However, the in situ structure and assembly mechanism of MacAB-TolC remain unclear. Here, we resolve the in situ structures of the MacAB-TolC efflux pump in Escherichia coli by electron cryo-tomography and subtomogram averaging. In the cells without antibiotic treatment, we observe a fully assembled MacAB-TolC pump. When Escherichia coli cells are treated with erythromycin, in addition to the tripartite pumps, we also discover the emergence of MacA-TolC subcomplexes without MacB, indicating flexible binding of MacB in the presence of an antibiotic substrate, which is further validated by in vivo photo-crosslinking results. Together, our data suggest the in situ assembly process of MacAB-TolC starts from the formation of MacA-TolC subcomplex, and provides insights into the design of efflux pump inhibitors.
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