ArticleNature communications2021
Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 99 citations in OpenAlex.
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- Immune protection and persistence in Pseudomonas aeruginosa infections by pyruvate cross-feeding.Nature communications · 2026Article
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- Mycobacterium tuberculosis assembles a unique hexameric E2p core of the pyruvate dehydrogenase complex.The Journal of biological chemistry · 2026Article
- The cellular esterase FrmB controls metabolic homeostasis and small colony variant formation inbioRxiv : the preprint server for biology · 2026Article
- NADH-Reductive Stress Induced by Dihydrolipoamide Dehydrogenase Activation Contributes to Cuproptosis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
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- Transcriptional analysis of genes associated with glycolysis in Streptomyces coelicolor M145.International microbiology : the official journal of the Spanish Society for Microbiology · 2025Article
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- NHC-Mediated Radical Acylation Catalyzed by Thiamine- and Flavin-Dependent Enzymes.Journal of the American Chemical Society · 2025Article
- DLAT activates EMT to promote HCC metastasis by regulating GLUT1-mediated aerobic glycolysis.Molecular medicine (Cambridge, Mass.) · 2025Article
- Rhizobacteria protective hydrogel to promote plant growth and adaption to acidic soil.Nature communications · 2025Article
- Dynamics of the mammalian pyruvate dehydrogenase complex revealed by in-situ structural analysis.Nature communications · 2025Article
- Copper metabolism and cuproptosis: broad perspectives in the treatment of hepatocellular carcinoma.Frontiers in oncology · 2025Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pyruvate dehydrogenase complex (PDHc) links glycolysis to the citric acid cycle by converting pyruvate into acetyl-coenzyme A. PDHc encompasses three enzymatically active subunits, namely pyruvate dehydrogenase, dihydrolipoyl transacetylase, and dihydrolipoyl dehydrogenase. Dihydrolipoyl transacetylase is a multidomain protein comprising a varying number of lipoyl domains, a peripheral subunit-binding domain, and a catalytic domain. It forms the structural core of the complex, provides binding sites for the other enzymes, and shuffles reaction intermediates between the active sites through covalently bound lipoyl domains. The molecular mechanism by which this shuttling occurs has remained elusive. Here, we report a cryo-EM reconstruction of the native E. coli dihydrolipoyl transacetylase core in a resting state. This structure provides molecular details of the assembly of the core and reveals how the lipoyl domains interact with the core at the active site.
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