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TitleStructural basis for EtfD-mediated coupling of β-oxidation and the respiratory chain in mycobacteria.
Journal, issue, pagesEMBO J, Year 2026
Publish dateMar 17, 2026
AuthorsGautier M Courbon / Vadim Makarov / Stewart T Cole / Dirk Schnapinger / Sabine Ehrt / John L Rubinstein /
PubMed AbstractTargeting β-oxidation has been proposed as a strategy for shortening tuberculosis (TB) treatment by killing non-replicating Mycobacterium tuberculosis within granulomas where the pathogen relies on ...Targeting β-oxidation has been proposed as a strategy for shortening tuberculosis (TB) treatment by killing non-replicating Mycobacterium tuberculosis within granulomas where the pathogen relies on host-derived lipids. The protein EtfD is thought to couple β-oxidation of fatty acids with the respiratory chain in mycobacteria. However, the structure of EtfD is not known and, as the presumed link between two complex processes, its activity has been difficult to measure, impeding its exploitation as a drug target. Here we show that Mycobacterium smegmatis, a fast growing and nonpathogenic model for M. tuberculosis, relies on EtfD for extracting energy from β-oxidation. The electron cryomicroscopy structure of M. smegmatis EtfD reveals an unusual linear [3Fe-4S] cluster that has not been seen in other protein structures, and suggests how EtfD transfers electrons from β-oxidation to the respiratory chain. We devised an assay that couples EtfD activity to a fluorescent readout of proton pumping by the respiratory chain, which can be used to identify compounds that block mycobacteria from using β-oxidation to power oxidative phosphorylation.
External linksEMBO J / PubMed:41844842
MethodsEM (single particle)
Resolution2.8 - 3.2 Å
Structure data

70545

9ojn

EMDB-70545, PDB-9ojn:
Structure of Mycobacterium smegmatis EtfD
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-70546: CryoEM map of Mycobacterium smegmatis EtfD cytosolic region
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-MQ9:
MENAQUINONE-9

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-9S8:
Non-cubane [4Fe-4S]-cluster

PDB-1cbx:
CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN CARBOXYPEPTIDASE A AND THE BIPRODUCT ANALOG INHIBITOR L-BENZYLSUCCINATE AT 2.0 ANGSTROMS RESOLUTION

Source
  • mycolicibacterium smegmatis mc2 155 (bacteria)
KeywordsOXIDOREDUCTASE / membrane protein / electron transport chain / beta oxidation

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