ArticleNature communications2020
Arrangement and symmetry of the fungal E3BP-containing core of the pyruvate dehydrogenase complex.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
- Mycobacterium tuberculosis assembles a unique hexameric E2p core of the pyruvate dehydrogenase complex.The Journal of biological chemistry · 2026Article
- Sspdhx Related to the Development and Virulence of Sclerotinia sclerotiorum Represents a Potential RNAi Target for Controlling Sclerotinia Disease.Molecular plant pathology · 2026Article
- The Pyruvate Dehydrogenase Complex: A 90-Year-Old Enigma Shaping the Future of Structural Enzymology.Advances in experimental medicine and biology · 2026Review
- Dynamics of the mammalian pyruvate dehydrogenase complex revealed by in-situ structural analysis.Nature communications · 2025Article
- Combined analysis of proteomics and metabolism reveals critical roles of oxidoreductase activity in mushrooms stimulated by wolfberry and sea buckthorn substrates.Frontiers in nutrition · 2025Article
- Comparative Analysis of Symmetry Parameters in the E2 Inner Core of the Pyruvate Dehydrogenase Complex.International journal of molecular sciences · 2024Article
- Dimerization of a 5-kDa domain defines the architecture of the 5-MDa gammaproteobacterial pyruvate dehydrogenase complex.Science advances · 2024Article
- Mitochondrial Alpha-Keto Acid Dehydrogenase Complexes: Recent Developments on Structure and Function in Health and Disease.Sub-cellular biochemistry · 2024Review
- A robust normalized local filter to estimate compositional heterogeneity directly from cryo-EM maps.Nature communications · 2023Article
- High resolution cryo-EM and crystallographic snapshots of the actinobacterial two-in-one 2-oxoglutarate dehydrogenase.Nature communications · 2023Article
- The structure and evolutionary diversity of the fungal E3-binding protein.Communications biology · 2023Article
- Structures and comparison of endogenous 2-oxoglutarate and pyruvate dehydrogenase complexes from bovine kidney.Cell discovery · 2022Article
- Simulations of Pathogenic E1α Variants: Allostery and Impact on Pyruvate Dehydrogenase Complex-E1 Structure and Function.Journal of chemical information and modeling · 2022Article
- Singapore Grouper Iridovirus Induces Glucose Metabolism in Infected Cells by Activation of Mammalian Target of Rapamycin Signaling.Frontiers in microbiology · 2022Article
- Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction.Nature communications · 2021Article
- Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion.Nature communications · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pyruvate dehydrogenase complex (PDC) is a multienzyme complex central to aerobic respiration, connecting glycolysis to mitochondrial oxidation of pyruvate. Similar to the E3-binding protein (E3BP) of mammalian PDC, PX selectively recruits E3 to the fungal PDC, but its divergent sequence suggests a distinct structural mechanism. Here, we report reconstructions of PDC from the filamentous fungus Neurospora crassa by cryo-electron microscopy, where we find protein X (PX) interior to the PDC core as opposed to substituting E2 core subunits as in mammals. Steric occlusion limits PX binding, resulting in predominantly tetrahedral symmetry, explaining previous observations in Saccharomyces cerevisiae. The PX-binding site is conserved in (and specific to) fungi, and complements possible C-terminal binding motifs in PX that are absent in mammalian E3BP. Consideration of multiple symmetries thus reveals a differential structural basis for E3BP-like function in fungal PDC.
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