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Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion

Biology

Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion

J. Škerlová, J. Berndtsson, et al.

This groundbreaking research reveals the intricate workings of the pyruvate dehydrogenase complex in *E. coli*, showcasing a cryo-EM reconstruction that uncovers the assembly and dynamics of dihydrolipoyl transacetylase. Conducted by Jana Škerlová, Jens Berndtsson, Hendrik Nolte, Martin Ott, and Pål Stenmark, this study sheds light on the active site's substrate shuttling mechanism.

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Playback language: English
Abstract
The pyruvate dehydrogenase complex (PDHc) links glycolysis to the citric acid cycle. This study reports a cryo-EM reconstruction of the native *E. coli* dihydrolipoyl transacetylase core in a resting state, providing molecular details of its assembly and revealing how lipoyl domains interact with the core at the active site, elucidating the mechanism of substrate shuttling.
Publisher
Nature Communications
Published On
Sep 06, 2021
Authors
Jana Škerlová, Jens Berndtsson, Hendrik Nolte, Martin Ott, Pål Stenmark
Tags
pyruvate dehydrogenase
cryo-EM
E. coli
dihydrolipoyl transacetylase
molecular assembly

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