ArticleNature communications2024
Structures of the Mycobacterium tuberculosis efflux pump EfpA reveal the mechanisms of transport and inhibition.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Deletion of MSMEG_3118, an ABC Transporter Family Protein in Mycobacterium smegmatis Alters Lipids Profile and Drug Susceptibility.Current microbiology · 2026Article
- Comparative Biological and Functional Profiling of Single-Position Cysteine Substitutions in the HNP-1-Derived Peptide Pep-H AgainstAntibiotics (Basel, Switzerland) · 2026Article
- Designing Antibiotics with Inherent Resistance to Efflux as a Strategy to Revive Discovery against Multidrug-Resistant Pathogens.Journal of medicinal chemistry · 2026Article
- Cryo-EM Structure of the FtsH Periplasmic Domain Reveals Functional Dynamics.ACS chemical biology · 2026Article
- Diverse regulation of functional dimerization of a sugar transporter by different interfacial lipids.Nature communications · 2026Article
- Structural basis of G6P/Pi transport and inhibition in SLC37A4.Nature structural & molecular biology · 2026Article
- Verapamil Suppresses the Development of Resistance Against Anti-Tuberculosis Drugs in Mycobacteria.International journal of molecular sciences · 2025Article
- Conformational cycle and small-molecule inhibition mechanism of a plant ABCB transporter in lipid membranes.Science advances · 2025Article
- Risk factors associated with morbidity and unfavorable treatment outcome in drug-resistant pulmonary tuberculosis: a case-control study.Precision clinical medicine · 2025Article
- Structure and inhibition mechanisms of Mycobacterium tuberculosis essential transporter efflux protein A.Nature communications · 2025Article
- Structure and function ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
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10 authors.
Funding
Abstract
As the first identified multidrug efflux pump in Mycobacterium tuberculosis (Mtb), EfpA is an essential protein and promising drug target. However, the functional and inhibitory mechanisms of EfpA are poorly understood. Here we report cryo-EM structures of EfpA in outward-open conformation, either bound to three endogenous lipids or the inhibitor BRD-8000.3. Three lipids inside EfpA span from the inner leaflet to the outer leaflet of the membrane. BRD-8000.3 occupies one lipid site at the level of inner membrane leaflet, competitively inhibiting lipid binding. EfpA resembles the related lysophospholipid transporter MFSD2A in both overall structure and lipid binding sites and may function as a lipid flippase. Combining AlphaFold-predicted EfpA structure, which is inward-open, we propose a complete conformational transition cycle for EfpA. Together, our results provide a structural and mechanistic foundation to comprehend EfpA function and develop EfpA-targeting anti-TB drugs.
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