Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1

Abstract Tyrosylprotein sulfotransferases (TPSTs) are enzymes that catalyze post-translational tyrosine sulfation of proteins. In humans, there are only two TPST isoforms, designated TPST1 and TPST2. In a previous study, we reported the crystal structure of TPST2, which revealed the catalytic mechan...

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Autores principales:	Shinnosuke Tanaka, Toshiaki Nishiyori, Hidetaka Kojo, Reo Otsubo, Moe Tsuruta, Katsuhisa Kurogi, Ming-Cheh Liu, Masahito Suiko, Yoichi Sakakibara, Yoshimitsu Kakuta
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5c636a709fdf4f76a0002010547b98a0
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spelling	oai:doaj.org-article:5c636a709fdf4f76a0002010547b98a02021-12-02T15:04:52ZStructural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-110.1038/s41598-017-07141-82045-2322https://doaj.org/article/5c636a709fdf4f76a0002010547b98a02017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-07141-8https://doaj.org/toc/2045-2322Abstract Tyrosylprotein sulfotransferases (TPSTs) are enzymes that catalyze post-translational tyrosine sulfation of proteins. In humans, there are only two TPST isoforms, designated TPST1 and TPST2. In a previous study, we reported the crystal structure of TPST2, which revealed the catalytic mechanism of the tyrosine sulfation reaction. However, detailed molecular mechanisms underlying how TPSTs catalyse a variety of substrate proteins with different efficiencies and how TPSTs catalyze the sulfation of multiple tyrosine residues in a substrate protein remain unresolved. Here, we report two crystal structures of the human TPST1 complexed with two substrate peptides that are catalysed by human TPST1 with significantly different efficiencies. The distinct binding modes found in the two complexes provide insight into the sulfation mechanism for these substrates. The present study provides valuable information describing the molecular mechanism of post-translational protein modifications catalysed by TPSTs.Shinnosuke TanakaToshiaki NishiyoriHidetaka KojoReo OtsuboMoe TsurutaKatsuhisa KurogiMing-Cheh LiuMasahito SuikoYoichi SakakibaraYoshimitsu KakutaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shinnosuke Tanaka Toshiaki Nishiyori Hidetaka Kojo Reo Otsubo Moe Tsuruta Katsuhisa Kurogi Ming-Cheh Liu Masahito Suiko Yoichi Sakakibara Yoshimitsu Kakuta Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1
description	Abstract Tyrosylprotein sulfotransferases (TPSTs) are enzymes that catalyze post-translational tyrosine sulfation of proteins. In humans, there are only two TPST isoforms, designated TPST1 and TPST2. In a previous study, we reported the crystal structure of TPST2, which revealed the catalytic mechanism of the tyrosine sulfation reaction. However, detailed molecular mechanisms underlying how TPSTs catalyse a variety of substrate proteins with different efficiencies and how TPSTs catalyze the sulfation of multiple tyrosine residues in a substrate protein remain unresolved. Here, we report two crystal structures of the human TPST1 complexed with two substrate peptides that are catalysed by human TPST1 with significantly different efficiencies. The distinct binding modes found in the two complexes provide insight into the sulfation mechanism for these substrates. The present study provides valuable information describing the molecular mechanism of post-translational protein modifications catalysed by TPSTs.
format	article
author	Shinnosuke Tanaka Toshiaki Nishiyori Hidetaka Kojo Reo Otsubo Moe Tsuruta Katsuhisa Kurogi Ming-Cheh Liu Masahito Suiko Yoichi Sakakibara Yoshimitsu Kakuta
author_facet	Shinnosuke Tanaka Toshiaki Nishiyori Hidetaka Kojo Reo Otsubo Moe Tsuruta Katsuhisa Kurogi Ming-Cheh Liu Masahito Suiko Yoichi Sakakibara Yoshimitsu Kakuta
author_sort	Shinnosuke Tanaka
title	Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1
title_short	Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1
title_full	Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1
title_fullStr	Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1
title_full_unstemmed	Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1
title_sort	structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/5c636a709fdf4f76a0002010547b98a0
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Structural basis for the broad substrate specificity of the human tyrosylprotein sulfotransferase-1

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