Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism

Abstract Sulphotransferases are a diverse group of enzymes catalysing the transfer of a sulfuryl group from 3′-phosphoadenosine 5′-phosphosulphate (PAPS) to a broad range of secondary metabolites. They exist in all kingdoms of life. In Arabidopsis thaliana (L.) Heynh. twenty-two sulphotransferase (S...

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Autores principales:	Felix Hirschmann, Florian Krause, Petra Baruch, Igor Chizhov, Jonathan Wolf Mueller, Dietmar J. Manstein, Jutta Papenbrock, Roman Fedorov
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7759b0cf7dcd4567b7acaaa342f0ca1a
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spelling	oai:doaj.org-article:7759b0cf7dcd4567b7acaaa342f0ca1a2021-12-02T16:06:29ZStructural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism10.1038/s41598-017-04539-22045-2322https://doaj.org/article/7759b0cf7dcd4567b7acaaa342f0ca1a2017-06-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-04539-2https://doaj.org/toc/2045-2322Abstract Sulphotransferases are a diverse group of enzymes catalysing the transfer of a sulfuryl group from 3′-phosphoadenosine 5′-phosphosulphate (PAPS) to a broad range of secondary metabolites. They exist in all kingdoms of life. In Arabidopsis thaliana (L.) Heynh. twenty-two sulphotransferase (SOT) isoforms were identified. Three of those are involved in glucosinolate (Gl) biosynthesis, glycosylated sulphur-containing aldoximes containing chemically different side chains, whose break-down products are involved in stress response against herbivores, pathogens, and abiotic stress. To explain the differences in substrate specificity of desulpho (ds)-Gl SOTs and to understand the reaction mechanism of plant SOTs, we determined the first high-resolution crystal structure of the plant ds-Gl SOT AtSOT18 in complex with 3′-phosphoadenosine 5′-phosphate (PAP) alone and together with the Gl sinigrin. These new structural insights into the determination of substrate specificity were complemented by mutagenesis studies. The structure of AtSOT18 invigorates the similarity between plant and mammalian sulphotransferases, which illustrates the evolutionary conservation of this multifunctional enzyme family. We identified the essential residues for substrate binding and catalysis and demonstrated that the catalytic mechanism is conserved between human and plant enzymes. Our study indicates that the loop-gating mechanism is likely to be a source of the substrate specificity in plants.Felix HirschmannFlorian KrausePetra BaruchIgor ChizhovJonathan Wolf MuellerDietmar J. MansteinJutta PapenbrockRoman FedorovNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Felix Hirschmann Florian Krause Petra Baruch Igor Chizhov Jonathan Wolf Mueller Dietmar J. Manstein Jutta Papenbrock Roman Fedorov Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism
description	Abstract Sulphotransferases are a diverse group of enzymes catalysing the transfer of a sulfuryl group from 3′-phosphoadenosine 5′-phosphosulphate (PAPS) to a broad range of secondary metabolites. They exist in all kingdoms of life. In Arabidopsis thaliana (L.) Heynh. twenty-two sulphotransferase (SOT) isoforms were identified. Three of those are involved in glucosinolate (Gl) biosynthesis, glycosylated sulphur-containing aldoximes containing chemically different side chains, whose break-down products are involved in stress response against herbivores, pathogens, and abiotic stress. To explain the differences in substrate specificity of desulpho (ds)-Gl SOTs and to understand the reaction mechanism of plant SOTs, we determined the first high-resolution crystal structure of the plant ds-Gl SOT AtSOT18 in complex with 3′-phosphoadenosine 5′-phosphate (PAP) alone and together with the Gl sinigrin. These new structural insights into the determination of substrate specificity were complemented by mutagenesis studies. The structure of AtSOT18 invigorates the similarity between plant and mammalian sulphotransferases, which illustrates the evolutionary conservation of this multifunctional enzyme family. We identified the essential residues for substrate binding and catalysis and demonstrated that the catalytic mechanism is conserved between human and plant enzymes. Our study indicates that the loop-gating mechanism is likely to be a source of the substrate specificity in plants.
format	article
author	Felix Hirschmann Florian Krause Petra Baruch Igor Chizhov Jonathan Wolf Mueller Dietmar J. Manstein Jutta Papenbrock Roman Fedorov
author_facet	Felix Hirschmann Florian Krause Petra Baruch Igor Chizhov Jonathan Wolf Mueller Dietmar J. Manstein Jutta Papenbrock Roman Fedorov
author_sort	Felix Hirschmann
title	Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism
title_short	Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism
title_full	Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism
title_fullStr	Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism
title_full_unstemmed	Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism
title_sort	structural and biochemical studies of sulphotransferase 18 from arabidopsis thaliana explain its substrate specificity and reaction mechanism
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/7759b0cf7dcd4567b7acaaa342f0ca1a
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Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism

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