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Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2021 Nov 30; Vol. 118 (48). - Publication Year :
- 2021
-
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 odhA gene coding for both the decarboxylase and the acyltransferase domains on the same polypetide, is spread over Actinobacteria and reflects the association of PDH and ODH into a single physical complex. Considering the central role of the pyruvate and 2-oxoglutarate nodes in central metabolism, our findings pave the way to both therapeutic and metabolic engineering applications.<br />Competing Interests: The authors declare no competing interest.
- Subjects :
- Bacteria metabolism
Biochemical Phenomena
Computational Biology
Crystallography, X-Ray
Kinetics
Molecular Conformation
Mycobacterium tuberculosis metabolism
Plasmids metabolism
Pyruvic Acid
Actinobacteria metabolism
Ketoglutarate Dehydrogenase Complex genetics
Pyruvate Dehydrogenase Complex metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1091-6490
- Volume :
- 118
- Issue :
- 48
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 34819376
- Full Text :
- https://doi.org/10.1073/pnas.2112107118