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Structure paper

TitleStructural basis of siderophore export and drug efflux by Mycobacterium tuberculosis.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 1934, Year 2025
Publish dateFeb 24, 2025
AuthorsJennifer C Earp / Alisa A Garaeva / Virginia Meikle / Michael Niederweis / Markus A Seeger /
PubMed AbstractTo replicate and cause disease, Mycobacterium tuberculosis secretes siderophores called mycobactins to scavenge iron from the human host. Two closely related transporters, MmpL4 and MmpL5, are ...To replicate and cause disease, Mycobacterium tuberculosis secretes siderophores called mycobactins to scavenge iron from the human host. Two closely related transporters, MmpL4 and MmpL5, are required for mycobactin secretion and drug efflux. In clinical strains, overproduction of MmpL5 confers resistance towards bedaquiline and clofazimine, key drugs to combat multidrug resistant tuberculosis. Here, we present cryogenic-electron microscopy structures of MmpL4 and identify a mycobactin binding site, which is accessible from the cytosol and also required for bedaquiline efflux. An unusual coiled-coil domain predicted to extend 130 Å into the periplasm is essential for mycobactin and bedaquiline efflux by MmpL4 and MmpL5. The mycobacterial acyl carrier protein MbtL forms a complex with MmpL4, indicating that mycobactin synthesis and export are coupled. Thus, MmpL4 and MmpL5 constitute the core components of a unique multi-subunit machinery required for iron acquisition and drug efflux by M. tuberculosis.
External linksNat Commun / PubMed:39994240 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 6.3 Å
Structure data

51366

9gi0

EMDB-51366, PDB-9gi0:
Truncated MmpL4 in detergent
Method: EM (single particle) / Resolution: 3.0 Å

51368

9gi2

EMDB-51368, PDB-9gi2:
Truncated MmpL4 in nanodiscs in absence of substrate
Method: EM (single particle) / Resolution: 3.4 Å

51369

9gi3

EMDB-51369, PDB-9gi3:
Truncated MmpL4 in nanodiscs in the presence of desferrated mycobactin
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-51370: Full-length MmpL4 in complex with the synthetic nanobody Sb09 and the E. coli acyl carrier protein
Method: EM (single particle) / Resolution: 6.3 Å

EMDB-51371: Truncated MmpL4 mutant R375E/R383E.
Method: EM (single particle) / Resolution: 5.1 Å

Chemicals

ChemComp-PEE:
1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE, phospholipid*YM

PDB-1il5:
STRUCTURE OF RICIN A CHAIN BOUND WITH INHIBITOR 2,5-DIAMINO-4,6-DIHYDROXYPYRIMIDINE (DDP)

Source
  • mycobacterium tuberculosis (bacteria)
  • escherichia coli mc1061 (bacteria)
KeywordsMEMBRANE PROTEIN / RND superfamily MmpL family Siderophore export Drug resistance Acyl carrier protein

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