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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Auteurs principaux:	Jana Škerlová, Jens Berndtsson, Hendrik Nolte, Martin Ott, Pål Stenmark
Format:	article
Langue:	EN
Publié:	Nature Portfolio 2021
Sujets:	Science Q
Accès en ligne:	https://doaj.org/article/3ce4dfc9c80943b38a2d9c01e7957c65
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spelling	oai:doaj.org-article:3ce4dfc9c80943b38a2d9c01e7957c652021-12-02T17:19:40ZStructure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion10.1038/s41467-021-25570-y2041-1723https://doaj.org/article/3ce4dfc9c80943b38a2d9c01e7957c652021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25570-yhttps://doaj.org/toc/2041-1723The 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.Jana ŠkerlováJens BerndtssonHendrik NolteMartin OttPål StenmarkNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jana Škerlová Jens Berndtsson Hendrik Nolte Martin Ott Pål Stenmark Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion
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.
format	article
author	Jana Škerlová Jens Berndtsson Hendrik Nolte Martin Ott Pål Stenmark
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 Portfolio
publishDate	2021
url	https://doaj.org/article/3ce4dfc9c80943b38a2d9c01e7957c65
work_keys_str_mv	AT janaskerlova structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion AT jensberndtsson structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion AT hendriknolte structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion AT martinott structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion AT palstenmark structureofthenativepyruvatedehydrogenasecomplexrevealsthemechanismofsubstrateinsertion
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Structure of the native pyruvate dehydrogenase complex reveals the mechanism of substrate insertion

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