Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex.
Actinobacteria
/ metabolism
Bacteria
/ metabolism
Biochemical Phenomena
Computational Biology
Crystallography, X-Ray
Ketoglutarate Dehydrogenase Complex
/ genetics
Kinetics
Molecular Conformation
Mycobacterium tuberculosis
/ metabolism
Plasmids
/ metabolism
Pyruvate Dehydrogenase Complex
/ metabolism
Pyruvic Acid
Actinobacteria
central metabolism
integrative structural biology
macromolecular complexes
pyruvate dehydrogenase
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
30 11 2021
30 11 2021
Historique:
accepted:
13
10
2021
entrez:
25
11
2021
pubmed:
26
11
2021
medline:
28
12
2021
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 34819376
pii: 2112107118
doi: 10.1073/pnas.2112107118
pmc: PMC8640841
pii:
doi:
Substances chimiques
Pyruvate Dehydrogenase Complex
0
Pyruvic Acid
8558G7RUTR
Ketoglutarate Dehydrogenase Complex
EC 1.2.4.2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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