Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme

Cyclohexadienyl dehydratase (CDT) evolved from a cationic amino acid binding protein ancestor without enzymatic activity (AncCDT-1) via a series of intermediates. Here, the authors combine EPR, X-ray crystallography and MD simulations to study the structural dynamics of these evolutionary intermedia...

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Autores principales:	Joe A. Kaczmarski, Mithun C. Mahawaththa, Akiva Feintuch, Ben E. Clifton, Luke A. Adams, Daniella Goldfarb, Gottfried Otting, Colin J. Jackson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c19f20f6641e4d50a18da243f7703954
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spelling	oai:doaj.org-article:c19f20f6641e4d50a18da243f77039542021-12-02T14:16:14ZAltered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme10.1038/s41467-020-19695-92041-1723https://doaj.org/article/c19f20f6641e4d50a18da243f77039542020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19695-9https://doaj.org/toc/2041-1723Cyclohexadienyl dehydratase (CDT) evolved from a cationic amino acid binding protein ancestor without enzymatic activity (AncCDT-1) via a series of intermediates. Here, the authors combine EPR, X-ray crystallography and MD simulations to study the structural dynamics of these evolutionary intermediates and observe that they predominantly populate catalytically unproductive conformations, while CDT exclusively samples catalytically relevant compact states, and which reveals how the conformational landscape changes along the evolutionary trajectory.Joe A. KaczmarskiMithun C. MahawaththaAkiva FeintuchBen E. CliftonLuke A. AdamsDaniella GoldfarbGottfried OttingColin J. JacksonNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Joe A. Kaczmarski Mithun C. Mahawaththa Akiva Feintuch Ben E. Clifton Luke A. Adams Daniella Goldfarb Gottfried Otting Colin J. Jackson Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme
description	Cyclohexadienyl dehydratase (CDT) evolved from a cationic amino acid binding protein ancestor without enzymatic activity (AncCDT-1) via a series of intermediates. Here, the authors combine EPR, X-ray crystallography and MD simulations to study the structural dynamics of these evolutionary intermediates and observe that they predominantly populate catalytically unproductive conformations, while CDT exclusively samples catalytically relevant compact states, and which reveals how the conformational landscape changes along the evolutionary trajectory.
format	article
author	Joe A. Kaczmarski Mithun C. Mahawaththa Akiva Feintuch Ben E. Clifton Luke A. Adams Daniella Goldfarb Gottfried Otting Colin J. Jackson
author_facet	Joe A. Kaczmarski Mithun C. Mahawaththa Akiva Feintuch Ben E. Clifton Luke A. Adams Daniella Goldfarb Gottfried Otting Colin J. Jackson
author_sort	Joe A. Kaczmarski
title	Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme
title_short	Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme
title_full	Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme
title_fullStr	Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme
title_full_unstemmed	Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme
title_sort	altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/c19f20f6641e4d50a18da243f7703954
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Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme

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