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TitleMycobacterium tuberculosis assembles a unique hexameric E2p core of the pyruvate dehydrogenase complex.
Journal, issue, pagesJ Biol Chem, Page 111284, Year 2026
Publish dateFeb 12, 2026
AuthorsHao-Chi Hsu / Isabelle Bonnet / Ruslana Bryk / Huilin Li /
PubMed AbstractThe pyruvate dehydrogenase complex (PDHc) is a universally conserved multienzyme system that converts pyruvate into acetyl-CoA for entry into the TCA cycle and for NADH production. Its central ...The pyruvate dehydrogenase complex (PDHc) is a universally conserved multienzyme system that converts pyruvate into acetyl-CoA for entry into the TCA cycle and for NADH production. Its central scaffold, the dihydrolipoyl transacetylase (E2p), forms an oligomeric inner core that recruits pyruvate dehydrogenase (E1p) and dihydrolipoyl dehydrogenase (E3). All previously characterized PDHc assemblies adopt either an octahedral 24-mer or an icosahedral 60-mer E2p core, each constructed from trimeric building blocks. We recently showed that the Mycobacterium tuberculosis (Mtb) E2p protein DlaT also functions as the core of the pathogen's peroxynitrite reductase/peroxidase (PNR/P) complex. Here, using cryo-EM, we demonstrate that DlaT assembles into discrete hexamers and dodecamers at micromolar concentrations, which approximate intracellular DlaT concentrations in Mtb. Structure-guided mutagenesis combined with in vitro activity assays indicate that the hexamer represents the functional E2p core of the Mtb PDHc. This noncanonical architecture arises from unique interfaces between DlaT trimers that preclude formation of the classic spherical 24- or 60-mer structures. We propose that this specialized E2p organization enables Mtb to regulate metabolic activities and to remodel the E2p core for engagement in the PNR/P antioxidant pathway under stress. Our findings reveal an unexpected diversity in PDHc architecture and uncover a distinct organization principle for the core metabolic complex in mycobacteria.
External linksJ Biol Chem / PubMed:41690596
MethodsEM (single particle)
Resolution2.51 - 4.51 Å
Structure data

72630

9y6t

EMDB-72630: Cryo-EM map of Mycobacterium tuberculosis pyruvate dehydrogenase complex E2p core subunit DlaT in a hexamer state
PDB-9y6t: Structure of Mycobacterium tuberculosis pyruvate dehydrogenase complex E2p core subunit DlaT in a hexamer state
Method: EM (single particle) / Resolution: 2.65 Å

72639

9y72

EMDB-72639: Cryo-EM map of Mycobacterium tuberculosis pyruvate dehydrogenase complex E2p core subunit DlaT in a two-hexamer state
PDB-9y72: Structure of Mycobacterium tuberculosis pyruvate dehydrogenase complex E2p core subunit DlaT in a two-hexamer state
Method: EM (single particle) / Resolution: 2.51 Å

72666

9y7v

EMDB-72666: Cryo-EM map of Mycobacterium tuberculosis pyruvate dehydrogenase complex E2p core subunit DlaT bound to coenzyme A in a hexamer state
PDB-9y7v: Structure of Mycobacterium tuberculosis pyruvate dehydrogenase complex E2p core subunit DlaT bound to coenzyme A in a hexamer state
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-72667: Cryo-EM map of Corynebacterium glutamicum pyruvate dehydrogenase complex E2p core in a trimer state
Method: EM (single particle) / Resolution: 4.51 Å

Chemicals

ChemComp-COA:
COENZYME A

Source
  • mycobacterium tuberculosis (bacteria)
  • Corynebacterium glutamicum (bacteria)
KeywordsTRANSFERASE / hexamer dihydrolipoamide acetyltransferase Mycobacterium tuberculosis pyruvate dehydrogenase complex / two-hexamer dihydrolipoamide acetyltransferase Mycobacterium tuberculosis pyruvate dehydrogenase complex / hexamer dihydrolipoamide acetyltransferase Mycobacterium tuberculosis Coenzyme A

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