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

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

The pyruvate dehydrogenase complex (PDHc) is a large multienzyme complex that converts pyruvate into acetyl-coenzyme A and in E. coli the core of the PDHc is formed by 24 copies of dihydrolipoyl transacetylase. Here, the authors present the cryo-EM structure of the E. coli dihydrolipoyl transacetyla...

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Main Authors: Jana Škerlová, Jens Berndtsson, Hendrik Nolte, Martin Ott, Pål Stenmark
Format: Article
Language:English
Published: Nature Publishing Group 2021-09-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-25570-y
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spelling doaj-3ce4dfc9c80943b38a2d9c01e7957c652021-09-12T11:45:52ZengNature Publishing GroupNature Communications2041-17232021-09-0112111010.1038/s41467-021-25570-yStructure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertionJana Škerlová0Jens Berndtsson1Hendrik Nolte2Martin Ott3Pål Stenmark4Department of Biochemistry and Biophysics, Stockholm UniversityDepartment of Biochemistry and Biophysics, Stockholm UniversityMax-Planck-Institute for Biology of AgeingDepartment of Biochemistry and Biophysics, Stockholm UniversityDepartment of Biochemistry and Biophysics, Stockholm UniversityThe pyruvate dehydrogenase complex (PDHc) is a large multienzyme complex that converts pyruvate into acetyl-coenzyme A and in E. coli the core of the PDHc is formed by 24 copies of dihydrolipoyl transacetylase. Here, the authors present the cryo-EM structure of the E. coli dihydrolipoyl transacetylase 24-mer core in a native resting state including lipoyl domains, and discuss the mechanism of substrate shuttling by the lipoyl domains.https://doi.org/10.1038/s41467-021-25570-y
collection DOAJ
language English
format Article
sources DOAJ
author Jana Škerlová
Jens Berndtsson
Hendrik Nolte
Martin Ott
Pål Stenmark
spellingShingle Jana Škerlová
Jens Berndtsson
Hendrik Nolte
Martin Ott
Pål Stenmark
Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
Nature Communications
author_facet Jana Škerlová
Jens Berndtsson
Hendrik Nolte
Martin Ott
Pål Stenmark
author_sort Jana Škerlová
title Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
title_short Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
title_full Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
title_fullStr Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
title_full_unstemmed Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
title_sort structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-09-01
description The pyruvate dehydrogenase complex (PDHc) is a large multienzyme complex that converts pyruvate into acetyl-coenzyme A and in E. coli the core of the PDHc is formed by 24 copies of dihydrolipoyl transacetylase. Here, the authors present the cryo-EM structure of the E. coli dihydrolipoyl transacetylase 24-mer core in a native resting state including lipoyl domains, and discuss the mechanism of substrate shuttling by the lipoyl domains.
url https://doi.org/10.1038/s41467-021-25570-y
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AT jensberndtsson structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion
AT hendriknolte structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion
AT martinott structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion
AT palstenmark structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion
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