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Structure of Mycobacterium tuberculosis pyruvate dehydrogenase complex E2p core subunit DlaT

ABSTRACT:

SUBMITTER: Hao-Chi Hsu 

PROVIDER: EMPIAR-13380 | biostudies-other |

REPOSITORIES: biostudies-other

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Mycobacterium tuberculosis assembles a unique hexameric E2p core of the pyruvate dehydrogenase complex.

Hsu Hao-Chi HC   Bonnet Isabelle I   Bryk Ruslana R   Li Huilin H  

The Journal of biological chemistry 20260212 4

The pyruvate dehydrogenase complex (PDHc) is a universally conserved multienzyme system that converts pyruvate into acetyl-CoA for entry into the tricarboxylic acid cycle and for NADH production. Its central scaffold, the dihydrolipoyl transacetylase (E2p), forms an oligomeric inner core that recruits pyruvate dehydrogenase (E1p) and dihydrolipoyl dehydrogenase (E3). All previously characterized PDHc assemblies adopt either an octahedral 24-mer or an icosahedral 60-mer E2p core, each constructed  ...[more]

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