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TitleMolecular basis of pyruvate transport and inhibition of the human mitochondrial pyruvate carrier.
Journal, issue, pagesSci Adv, Vol. 11, Issue 16, Page eadw1489, Year 2025
Publish dateApr 18, 2025
AuthorsMaximilian Sichrovsky / Denis Lacabanne / Jonathan J Ruprecht / Jessica J Rana / Klaudia Stanik / Mariangela Dionysopoulou / Alice P Sowton / Martin S King / Scott A Jones / Lee Cooper / Steven W Hardwick / Giulia Paris / Dimitri Y Chirgadze / Shujing Ding / Ian M Fearnley / Shane M Palmer / Els Pardon / Jan Steyaert / Vanessa Leone / Lucy R Forrest / Sotiria Tavoulari / Edmund R S Kunji /
PubMed AbstractThe mitochondrial pyruvate carrier transports pyruvate, produced by glycolysis from sugar molecules, into the mitochondrial matrix, as a crucial transport step in eukaryotic energy metabolism. The ...The mitochondrial pyruvate carrier transports pyruvate, produced by glycolysis from sugar molecules, into the mitochondrial matrix, as a crucial transport step in eukaryotic energy metabolism. The carrier is a drug target for the treatment of cancers, diabetes mellitus, neurodegeneration, and metabolic dysfunction-associated steatotic liver disease. We have solved the structure of the human MPC1L/MPC2 heterodimer in the inward- and outward-open states by cryo-electron microscopy, revealing its alternating access rocker-switch mechanism. The carrier has a central binding site for pyruvate, which contains an essential lysine and histidine residue, important for its ΔpH-dependent transport mechanism. We have also determined the binding poses of three chemically distinct inhibitor classes, which exploit the same binding site in the outward-open state by mimicking pyruvate interactions and by using aromatic stacking interactions.
External linksSci Adv / PubMed:40249800 / PubMed Central
MethodsEM (single particle)
Resolution3.65 - 3.92 Å
Structure data

51378

9giv

EMDB-51378, PDB-9giv:
Structure of the human mitochondrial pyruvate carrier inhibited by a UK5099-derivative
Method: EM (single particle) / Resolution: 3.65 Å

51379

9giw

EMDB-51379, PDB-9giw:
Structure of the human mitochondrial pyruvate carrier inhibited by zaprinast
Method: EM (single particle) / Resolution: 3.92 Å

51380

9gix

EMDB-51380, PDB-9gix:
Structure of the human mitochondrial pyruvate carrier in the apo-state
Method: EM (single particle) / Resolution: 3.65 Å

51381

9giy

EMDB-51381, PDB-9giy:
Structure of the human mitochondrial pyruvate carrier inhibited by mitoglitazone
Method: EM (single particle) / Resolution: 3.79 Å

Chemicals

PDB-1il4:
STRUCTURE OF RICIN A CHAIN BOUND WITH INHIBITOR 9-DEAZAGUANINE

PDB-1il3:
STRUCTURE OF RICIN A CHAIN BOUND WITH INHIBITOR 7-DEAZAGUANINE

ChemComp-LO7:
Mitoglitazone


PDB Unreleased entry

PDB-1imz: Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
  • escherichia coli k-12 (bacteria)
KeywordsMEMBRANE PROTEIN / transporter SLC54 pyruvate UK5099-derivative

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