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

Autor: Mirjam Czjzek, Anne S. Meyer, Van Thi Thanh Tran, Thuan Thi Nguyen, Thomas Roret, Nanna Rhein-Knudsen, Vy Ha Nguyen Tran, Jesper Holck, Thinh Duc Pham, Jan Muschiol, Hang Thi Thuy Cao, Maria Dalgaard Mikkelsen, Mateusz Jakub Lezyk
Přispěvatelé: Technical University of Denmark [Lyngby] (DTU), Vietnam Academy of Science and Technology (VAST), Station biologique de Roscoff (SBR), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2021
Předmět:
Zdroj: Scientific Reports
Scientific Reports, Nature Publishing Group, 2021, 11 (1), ⟨10.1038/s41598-021-98588-3⟩
Scientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
Mikkelsen, M D, Cao, H T T, Roret, T, Rhein-Knudsen, N, Holck, J, Tran, V T T, Nguyen, T T, Tran, V H N, Lezyk, M J, Muschiol, J, Pham, T D, Czjzek, M & Meyer, A S 2021, ' A novel thermostable prokaryotic fucoidan active sulfatase PsFucS1 with an unusual quaternary hexameric structure ', Scientific Reports, vol. 11, 19523 . https://doi.org/10.1038/s41598-021-98588-3
ISSN: 2045-2322
Popis: 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.
Databáze: OpenAIRE