ArticleStructure (London, England : 1993)2021
Cryo-EM structure and resistance landscape of M. tuberculosis MmpL3: An emergent therapeutic target.
Article in Structure (London, England : 1993), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Structure, assembly, and mechanism of the MmpL family of transporters.Microbiology and molecular biology reviews : MMBR · 2026Review
- Integrating computational and biological approaches for the discovery of putative MmpL3 inhibitors against Mycobacterium tuberculosis.Molecular diversity · 2026Article
- Gaining insights into MmpL3: combining structural and computational approaches to unlock transport and inhibitor-binding mechanisms.Acta crystallographica. Section D, Structural biology · 2026Article
- Combined computational and classical medicinal chemistry procedure to disclose novel pyrrole-based compounds as potential antituberculosis agents.Journal of computer-aided molecular design · 2026Article
- Bacterial cell envelope-targeting antibiotics.Nature reviews. Microbiology · 2026Review
- Structural elucidation of the hexameric MmpS4-MmpL4 complex frombioRxiv : the preprint server for biology · 2026Article
- Cryo-EM structures of mycobacteria MmpL5-AcpM complex.Science China. Life sciences · 2025Article
- Thienopyrimidine amide analogs target MmpL3 inAntimicrobial agents and chemotherapy · 2025Article
- MmpL12 transports lipooligosaccharides and impacts virulence inMicrobiology (Reading, England) · 2025Article
- Structural and functional analysis of theProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structures of MmpL complexes reveal the assembly and mechanism of this family of transporters.Science advances · 2025Article
- Investigating the unbinding mechanisms and kinetics of MmpL3 inhibitors: A computational study.Protein science : a publication of the Protein Society · 2025Article
- A coiled-coil domain triggers oligomerization of MmpL10, the mycobacterial transporter of trehalose polyphleate precursor.FEBS letters · 2025Article
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- Structural basis of siderophore export and drug efflux by Mycobacterium tuberculosis.Nature communications · 2025Article
- Article
- Developing novel indoles as antitubercular agents and simulated annealing-based analysis of their binding with MmpL3.Future medicinal chemistry · 2025Article
- Article
- Structural modeling and characterization of the Mycobacterium tuberculosis MmpL3 C-terminal domain.FEBS letters · 2024Article
- An open-access dashboard to interrogate the genetic diversity of Mycobacterium tuberculosis clinical isolates.Scientific reports · 2024Article
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7 authors.
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Abstract
Tuberculosis (TB) is the leading cause of death from a single infectious agent and in 2019 an estimated 10 million people worldwide contracted the disease. Although treatments for TB exist, continual emergence of drug-resistant variants necessitates urgent development of novel antituberculars. An important new target is the lipid transporter MmpL3, which is required for construction of the unique cell envelope that shields Mycobacterium tuberculosis (Mtb) from the immune system. However, a structural understanding of the mutations in Mtb MmpL3 that confer resistance to the many preclinical leads is lacking, hampering efforts to circumvent resistance mechanisms. Here, we present the cryoelectron microscopy structure of Mtb MmpL3 and use it to comprehensively analyze the mutational landscape of drug resistance. Our data provide a rational explanation for resistance variants local to the central drug binding site, and also highlight a potential alternative route to resistance operating within the periplasmic domain.
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