A rotary mechanism for allostery in bacterial hybrid malic enzymes

Bacterial malic enzymes (ME) transform malate to pyruvate. One group, hybrid ME enzymes, are regulated by acetyl-CoA, linking the enzyme activity to the metabolic state of the cell. Structures of a representative hybrid ME MaeB reveal large conformational rearrangements that provide insight into the...

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Autores principales:	Christopher John Harding, Ian Thomas Cadby, Patrick Joseph Moynihan, Andrew Lee Lovering
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5190409fbdc14f5b84ad4f155f6403ed
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spelling	oai:doaj.org-article:5190409fbdc14f5b84ad4f155f6403ed2021-12-02T14:29:04ZA rotary mechanism for allostery in bacterial hybrid malic enzymes10.1038/s41467-021-21528-22041-1723https://doaj.org/article/5190409fbdc14f5b84ad4f155f6403ed2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21528-2https://doaj.org/toc/2041-1723Bacterial malic enzymes (ME) transform malate to pyruvate. One group, hybrid ME enzymes, are regulated by acetyl-CoA, linking the enzyme activity to the metabolic state of the cell. Structures of a representative hybrid ME MaeB reveal large conformational rearrangements that provide insight into the mechanism of allosteric inhibition by acetyl-CoA.Christopher John HardingIan Thomas CadbyPatrick Joseph MoynihanAndrew Lee LoveringNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Christopher John Harding Ian Thomas Cadby Patrick Joseph Moynihan Andrew Lee Lovering A rotary mechanism for allostery in bacterial hybrid malic enzymes
description	Bacterial malic enzymes (ME) transform malate to pyruvate. One group, hybrid ME enzymes, are regulated by acetyl-CoA, linking the enzyme activity to the metabolic state of the cell. Structures of a representative hybrid ME MaeB reveal large conformational rearrangements that provide insight into the mechanism of allosteric inhibition by acetyl-CoA.
format	article
author	Christopher John Harding Ian Thomas Cadby Patrick Joseph Moynihan Andrew Lee Lovering
author_facet	Christopher John Harding Ian Thomas Cadby Patrick Joseph Moynihan Andrew Lee Lovering
author_sort	Christopher John Harding
title	A rotary mechanism for allostery in bacterial hybrid malic enzymes
title_short	A rotary mechanism for allostery in bacterial hybrid malic enzymes
title_full	A rotary mechanism for allostery in bacterial hybrid malic enzymes
title_fullStr	A rotary mechanism for allostery in bacterial hybrid malic enzymes
title_full_unstemmed	A rotary mechanism for allostery in bacterial hybrid malic enzymes
title_sort	rotary mechanism for allostery in bacterial hybrid malic enzymes
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/5190409fbdc14f5b84ad4f155f6403ed
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A rotary mechanism for allostery in bacterial hybrid malic enzymes

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