Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases

Rieske oxygenases are iron-dependent enzymes that catalyse C–H mono- and dihydroxylation reactions. Here, the authors characterise two cyanobacterial Rieske oxygenases, SxtT and GxtA that are involved in the biosynthesis of paralytic shellfish toxins and determine their substrate free and saxitoxin...

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Autores principales:	April L. Lukowski, Jianxin Liu, Jennifer Bridwell-Rabb, Alison R. H. Narayan
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b69e299e06b4475ab6229373dc78b546
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spelling	oai:doaj.org-article:b69e299e06b4475ab6229373dc78b5462021-12-02T17:47:17ZStructural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases10.1038/s41467-020-16729-02041-1723https://doaj.org/article/b69e299e06b4475ab6229373dc78b5462020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16729-0https://doaj.org/toc/2041-1723Rieske oxygenases are iron-dependent enzymes that catalyse C–H mono- and dihydroxylation reactions. Here, the authors characterise two cyanobacterial Rieske oxygenases, SxtT and GxtA that are involved in the biosynthesis of paralytic shellfish toxins and determine their substrate free and saxitoxin analog-bound crystal structures and by using mutagenesis experiments identify residues, which are important for substrate positioning and reaction selectivity.April L. LukowskiJianxin LiuJennifer Bridwell-RabbAlison R. H. NarayanNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q April L. Lukowski Jianxin Liu Jennifer Bridwell-Rabb Alison R. H. Narayan Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases
description	Rieske oxygenases are iron-dependent enzymes that catalyse C–H mono- and dihydroxylation reactions. Here, the authors characterise two cyanobacterial Rieske oxygenases, SxtT and GxtA that are involved in the biosynthesis of paralytic shellfish toxins and determine their substrate free and saxitoxin analog-bound crystal structures and by using mutagenesis experiments identify residues, which are important for substrate positioning and reaction selectivity.
format	article
author	April L. Lukowski Jianxin Liu Jennifer Bridwell-Rabb Alison R. H. Narayan
author_facet	April L. Lukowski Jianxin Liu Jennifer Bridwell-Rabb Alison R. H. Narayan
author_sort	April L. Lukowski
title	Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases
title_short	Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases
title_full	Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases
title_fullStr	Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases
title_full_unstemmed	Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases
title_sort	structural basis for divergent c–h hydroxylation selectivity in two rieske oxygenases
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b69e299e06b4475ab6229373dc78b546
work_keys_str_mv	AT aprilllukowski structuralbasisfordivergentchhydroxylationselectivityintworieskeoxygenases AT jianxinliu structuralbasisfordivergentchhydroxylationselectivityintworieskeoxygenases AT jenniferbridwellrabb structuralbasisfordivergentchhydroxylationselectivityintworieskeoxygenases AT alisonrhnarayan structuralbasisfordivergentchhydroxylationselectivityintworieskeoxygenases
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Structural basis for divergent C–H hydroxylation selectivity in two Rieske oxygenases

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