Structural insight into a CE15 esterase from the marine bacterial metagenome

Abstract The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previousl...

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Autores principales:	Concetta De Santi, Osman ABSM Gani, Ronny Helland, Adele Williamson
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/866378946e154b7289823b30b9e57bf9
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spelling	oai:doaj.org-article:866378946e154b7289823b30b9e57bf92021-12-02T15:05:30ZStructural insight into a CE15 esterase from the marine bacterial metagenome10.1038/s41598-017-17677-42045-2322https://doaj.org/article/866378946e154b7289823b30b9e57bf92017-12-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-17677-4https://doaj.org/toc/2045-2322Abstract The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-characterized fungal homologs, and resolves three large loop regions that are unique to this bacterial sub-clade. The catalytic triad of the bacterial CE15, which includes Asp 332 as its third member, closely resembles that of family 1 carbohydrate esterases (CE1), despite the overall lower structural similarity with members of this family. Two of the three loop regions form a subdomain that deepens the active site pocket and includes several basic residues that contribute to the high positive charge surrounding the active site. Docking simulations predict specific interactions with the sugar moiety of glucuronic-acid substrates, and with aromatically-substituted derivatives that serve as model compounds for the lignin-carbohydrate complex of plant cell walls. Molecular dynamics simulations indicate considerable flexibility of the sub-domain in the substrate-bound form, suggesting plasticity to accommodate different substrates is possible. The findings from this first reported structure of a bacterial member of the CE15 family provide insight into the basis of its broader substrate specificity.Concetta De SantiOsman ABSM GaniRonny HellandAdele WilliamsonNature 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 Concetta De Santi Osman ABSM Gani Ronny Helland Adele Williamson Structural insight into a CE15 esterase from the marine bacterial metagenome
description	Abstract The family 15 carbohydrate esterase (CE15) MZ0003, which derives from a marine Arctic metagenome, has a broader substrate scope than other members of this family. Here we report the crystal structure of MZ0003, which reveals that residues comprising the catalytic triad differ from previously-characterized fungal homologs, and resolves three large loop regions that are unique to this bacterial sub-clade. The catalytic triad of the bacterial CE15, which includes Asp 332 as its third member, closely resembles that of family 1 carbohydrate esterases (CE1), despite the overall lower structural similarity with members of this family. Two of the three loop regions form a subdomain that deepens the active site pocket and includes several basic residues that contribute to the high positive charge surrounding the active site. Docking simulations predict specific interactions with the sugar moiety of glucuronic-acid substrates, and with aromatically-substituted derivatives that serve as model compounds for the lignin-carbohydrate complex of plant cell walls. Molecular dynamics simulations indicate considerable flexibility of the sub-domain in the substrate-bound form, suggesting plasticity to accommodate different substrates is possible. The findings from this first reported structure of a bacterial member of the CE15 family provide insight into the basis of its broader substrate specificity.
format	article
author	Concetta De Santi Osman ABSM Gani Ronny Helland Adele Williamson
author_facet	Concetta De Santi Osman ABSM Gani Ronny Helland Adele Williamson
author_sort	Concetta De Santi
title	Structural insight into a CE15 esterase from the marine bacterial metagenome
title_short	Structural insight into a CE15 esterase from the marine bacterial metagenome
title_full	Structural insight into a CE15 esterase from the marine bacterial metagenome
title_fullStr	Structural insight into a CE15 esterase from the marine bacterial metagenome
title_full_unstemmed	Structural insight into a CE15 esterase from the marine bacterial metagenome
title_sort	structural insight into a ce15 esterase from the marine bacterial metagenome
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/866378946e154b7289823b30b9e57bf9
work_keys_str_mv	AT concettadesanti structuralinsightintoace15esterasefromthemarinebacterialmetagenome AT osmanabsmgani structuralinsightintoace15esterasefromthemarinebacterialmetagenome AT ronnyhelland structuralinsightintoace15esterasefromthemarinebacterialmetagenome AT adelewilliamson structuralinsightintoace15esterasefromthemarinebacterialmetagenome
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Structural insight into a CE15 esterase from the marine bacterial metagenome

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