A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure

Abstract Fucoidans are sulfated, fucose-rich marine polysaccharides primarily found in cell walls of brown seaweeds (macroalgae). Fucoidans are known to possess beneficial bioactivities depending on their structure and sulfation degree. Here, we report the first functional characterization and the f...

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Autores principales:	Maria Dalgaard Mikkelsen, Hang Thi Thuy Cao, Thomas Roret, Nanna Rhein-Knudsen, Jesper Holck, Van Thi Thanh Tran, Thuan Thi Nguyen, Vy Ha Nguyen Tran, Mateusz Jakub Lezyk, Jan Muschiol, Thinh Duc Pham, Mirjam Czjzek, Anne S. Meyer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/cc38177e7dd745e28e3da788539a2bda
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spelling	oai:doaj.org-article:cc38177e7dd745e28e3da788539a2bda2021-12-02T17:37:40ZA novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure10.1038/s41598-021-98588-32045-2322https://doaj.org/article/cc38177e7dd745e28e3da788539a2bda2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-98588-3https://doaj.org/toc/2045-2322Abstract Fucoidans are sulfated, fucose-rich marine polysaccharides primarily found in cell walls of brown seaweeds (macroalgae). Fucoidans are known to possess beneficial bioactivities depending on their structure and sulfation degree. Here, we report the first functional characterization and the first crystal structure of a prokaryotic sulfatase, PsFucS1, belonging to sulfatase subfamily S1_13, able to release sulfate from fucoidan oligosaccharides. PsFucS1 was identified in the genome of a Pseudoalteromonas sp. isolated from sea cucumber gut. PsFucS1 (57 kDa) is Ca2+ dependent and has an unusually high optimal temperature (68 °C) and thermostability. Further, the PsFucS1 displays a unique quaternary hexameric structure comprising a tight trimeric dimer complex. The structural data imply that this hexamer formation results from an uncommon interaction of each PsFucS1 monomer that is oriented perpendicular to the common dimer interface (~ 1500 Å2) that can be found in analogous sulfatases. The uncommon interaction involves interfacing (1246 Å2) through a bundle of α-helices in the N-terminal domain to form a trimeric ring structure. The high thermostability may be related to this unusual quaternary hexameric structure formation that is suggested to represent a novel protein thermostabilization mechanism.Maria Dalgaard MikkelsenHang Thi Thuy CaoThomas RoretNanna Rhein-KnudsenJesper HolckVan Thi Thanh TranThuan Thi NguyenVy Ha Nguyen TranMateusz Jakub LezykJan MuschiolThinh Duc PhamMirjam CzjzekAnne S. MeyerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Maria Dalgaard Mikkelsen Hang Thi Thuy Cao Thomas Roret Nanna Rhein-Knudsen Jesper Holck Van Thi Thanh Tran Thuan Thi Nguyen Vy Ha Nguyen Tran Mateusz Jakub Lezyk Jan Muschiol Thinh Duc Pham Mirjam Czjzek Anne S. Meyer A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure
description	Abstract Fucoidans are sulfated, fucose-rich marine polysaccharides primarily found in cell walls of brown seaweeds (macroalgae). Fucoidans are known to possess beneficial bioactivities depending on their structure and sulfation degree. Here, we report the first functional characterization and the first crystal structure of a prokaryotic sulfatase, PsFucS1, belonging to sulfatase subfamily S1_13, able to release sulfate from fucoidan oligosaccharides. PsFucS1 was identified in the genome of a Pseudoalteromonas sp. isolated from sea cucumber gut. PsFucS1 (57 kDa) is Ca2+ dependent and has an unusually high optimal temperature (68 °C) and thermostability. Further, the PsFucS1 displays a unique quaternary hexameric structure comprising a tight trimeric dimer complex. The structural data imply that this hexamer formation results from an uncommon interaction of each PsFucS1 monomer that is oriented perpendicular to the common dimer interface (~ 1500 Å2) that can be found in analogous sulfatases. The uncommon interaction involves interfacing (1246 Å2) through a bundle of α-helices in the N-terminal domain to form a trimeric ring structure. The high thermostability may be related to this unusual quaternary hexameric structure formation that is suggested to represent a novel protein thermostabilization mechanism.
format	article
author	Maria Dalgaard Mikkelsen Hang Thi Thuy Cao Thomas Roret Nanna Rhein-Knudsen Jesper Holck Van Thi Thanh Tran Thuan Thi Nguyen Vy Ha Nguyen Tran Mateusz Jakub Lezyk Jan Muschiol Thinh Duc Pham Mirjam Czjzek Anne S. Meyer
author_facet	Maria Dalgaard Mikkelsen Hang Thi Thuy Cao Thomas Roret Nanna Rhein-Knudsen Jesper Holck Van Thi Thanh Tran Thuan Thi Nguyen Vy Ha Nguyen Tran Mateusz Jakub Lezyk Jan Muschiol Thinh Duc Pham Mirjam Czjzek Anne S. Meyer
author_sort	Maria Dalgaard Mikkelsen
title	A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure
title_short	A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure
title_full	A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure
title_fullStr	A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure
title_full_unstemmed	A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure
title_sort	novel thermostable prokaryotic fucoidan active sulfatase psfucs1 with an unusual quaternary hexameric structure
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/cc38177e7dd745e28e3da788539a2bda
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A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure

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