ArticleProceedings of the National Academy of Sciences of the United States of America2021
Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Mycobacterium tuberculosis assembles a unique hexameric E2p core of the pyruvate dehydrogenase complex.The Journal of biological chemistry · 2026Article
- Molecular architecture of the mammalian 2-oxoglutarate dehydrogenase complex.Nature communications · 2024Article
- Dimerization of a 5-kDa domain defines the architecture of the 5-MDa gammaproteobacterial pyruvate dehydrogenase complex.Science advances · 2024Article
- Cellular localization of the hybrid pyruvate/2-oxoglutarate dehydrogenase complex in the actinobacteriumMicrobiology spectrum · 2023Article
- High resolution cryo-EM and crystallographic snapshots of the actinobacterial two-in-one 2-oxoglutarate dehydrogenase.Nature communications · 2023Article
- Characteristics of the GlnH and GlnX Signal Transduction Proteins Controlling PknG-Mediated Phosphorylation of OdhI and 2-Oxoglutarate Dehydrogenase Activity in Corynebacterium glutamicum.Microbiology spectrum · 2022Article
- Structures and comparison of endogenous 2-oxoglutarate and pyruvate dehydrogenase complexes from bovine kidney.Cell discovery · 2022Article
- Article
- How evolution dismantles and reassembles multienzyme complexes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Relevance of NADH Dehydrogenase and Alternative Two-Enzyme Systems for Growth ofFrontiers in bioengineering and biotechnology · 2020Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-oxoacid dehydrogenase complexes are large, tripartite enzymatic machineries carrying out key reactions in central metabolism. Extremely conserved across the tree of life, they have been, so far, all considered to be structured around a high-molecular weight hollow core, consisting of up to 60 subunits of the acyltransferase component. We provide here evidence that Actinobacteria break the rule by possessing an acetyltranferase component reduced to its minimally active, trimeric unit, characterized by a unique C-terminal helix bearing an actinobacterial specific insertion that precludes larger protein oligomerization. This particular feature, together with the presence of an
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