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Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum

Beta-glucosidases (β-glucosidases) have attracted considerable attention in recent years for use in various biotechnological applications. They are also essential enzymes for lignocellulose degradation in biofuel production. However, cost-effective biomass conversion requires the use of highly effic...

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Autores principales: Mohsin, Imran, Poudel, Nirmal, Li, Duo-Chuan, Papageorgiou, Anastassios C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6929035/
https://www.ncbi.nlm.nih.gov/pubmed/31783503
http://dx.doi.org/10.3390/ijms20235962
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author Mohsin, Imran
Poudel, Nirmal
Li, Duo-Chuan
Papageorgiou, Anastassios C.
author_facet Mohsin, Imran
Poudel, Nirmal
Li, Duo-Chuan
Papageorgiou, Anastassios C.
author_sort Mohsin, Imran
collection PubMed
description Beta-glucosidases (β-glucosidases) have attracted considerable attention in recent years for use in various biotechnological applications. They are also essential enzymes for lignocellulose degradation in biofuel production. However, cost-effective biomass conversion requires the use of highly efficient enzymes. Thus, the search for new enzymes as better alternatives of the currently available enzyme preparations is highly important. Thermophilic fungi are nowadays considered as a promising source of enzymes with improved stability. Here, the crystal structure of a family GH3 β-glucosidase from the thermophilic fungus Chaetomium thermophilum (CtBGL) was determined at a resolution of 2.99 Å. The structure showed the three-domain architecture found in other β-glucosidases with variations in loops and linker regions. The active site catalytic residues in CtBGL were identified as Asp287 (nucleophile) and Glu517 (acid/base). Structural comparison of CtBGL with Protein Data Bank (PDB)-deposited structures revealed variations among glycosylated Asn residues. The enzyme displayed moderate glycosylation compared to other GH3 family β-glucosidases with similar structure. A new glycosylation site at position Asn504 was identified in CtBGL. Moreover, comparison with respect to several thermostability parameters suggested that glycosylation and charged residues involved in electrostatic interactions may contribute to the stability of the enzyme at elevated temperatures. The reported CtBGL structure provides additional insights into the family GH3 enzymes and could offer new ideas for further improvements in β-glucosidases for more efficient use in biotechnological applications regarding cellulose degradation.
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spelling pubmed-69290352019-12-26 Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum Mohsin, Imran Poudel, Nirmal Li, Duo-Chuan Papageorgiou, Anastassios C. Int J Mol Sci Article Beta-glucosidases (β-glucosidases) have attracted considerable attention in recent years for use in various biotechnological applications. They are also essential enzymes for lignocellulose degradation in biofuel production. However, cost-effective biomass conversion requires the use of highly efficient enzymes. Thus, the search for new enzymes as better alternatives of the currently available enzyme preparations is highly important. Thermophilic fungi are nowadays considered as a promising source of enzymes with improved stability. Here, the crystal structure of a family GH3 β-glucosidase from the thermophilic fungus Chaetomium thermophilum (CtBGL) was determined at a resolution of 2.99 Å. The structure showed the three-domain architecture found in other β-glucosidases with variations in loops and linker regions. The active site catalytic residues in CtBGL were identified as Asp287 (nucleophile) and Glu517 (acid/base). Structural comparison of CtBGL with Protein Data Bank (PDB)-deposited structures revealed variations among glycosylated Asn residues. The enzyme displayed moderate glycosylation compared to other GH3 family β-glucosidases with similar structure. A new glycosylation site at position Asn504 was identified in CtBGL. Moreover, comparison with respect to several thermostability parameters suggested that glycosylation and charged residues involved in electrostatic interactions may contribute to the stability of the enzyme at elevated temperatures. The reported CtBGL structure provides additional insights into the family GH3 enzymes and could offer new ideas for further improvements in β-glucosidases for more efficient use in biotechnological applications regarding cellulose degradation. MDPI 2019-11-27 /pmc/articles/PMC6929035/ /pubmed/31783503 http://dx.doi.org/10.3390/ijms20235962 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Mohsin, Imran
Poudel, Nirmal
Li, Duo-Chuan
Papageorgiou, Anastassios C.
Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum
title Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum
title_full Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum
title_fullStr Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum
title_full_unstemmed Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum
title_short Crystal Structure of a GH3 β-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum
title_sort crystal structure of a gh3 β-glucosidase from the thermophilic fungus chaetomium thermophilum
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6929035/
https://www.ncbi.nlm.nih.gov/pubmed/31783503
http://dx.doi.org/10.3390/ijms20235962
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