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

Imran Mohsin; Anastassios C. Papageorgiou; Nirmal Poudel; Duo-Chuan Li

dc.contributor.authorImran Mohsin
dc.contributor.authorAnastassios C. Papageorgiou
dc.contributor.authorNirmal Poudel
dc.contributor.authorDuo-Chuan Li
dc.date.accessioned2022-10-28T12:31:19Z
dc.date.available2022-10-28T12:31:19Z
dc.identifier.urihttps://www.utupub.fi/handle/10024/160102
dc.description.abstractBeta-glucosidases (beta-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 beta-glucosidase from the thermophilic fungus Chaetomium thermophilum (CtBGL) was determined at a resolution of 2.99 angstrom. The structure showed the three-domain architecture found in other beta-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 beta-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 beta-glucosidases for more efficient use in biotechnological applications regarding cellulose degradation.
dc.language.isoen
dc.publisherMDPI
dc.titleCrystal Structure of a GH3 beta-Glucosidase from the Thermophilic Fungus Chaetomium thermophilum
dc.identifier.urnURN:NBN:fi-fe2021042824976
dc.relation.volume20
dc.contributor.organizationfi=PÄÄT Biokemia|en=PÄÄT Biochemistry|
dc.contributor.organizationfi=biotiedekeskuksen yhteiset|en=Biotiedekeskuksen yhteiset|
dc.contributor.organization-code2609200
dc.contributor.organization-code2606201
dc.converis.publication-id44148063
dc.converis.urlhttps://research.utu.fi/converis/portal/Publication/44148063
dc.identifier.eissn1422-0067
dc.identifier.jour-issn1661-6596
dc.okm.affiliatedauthorPoudel, Nirmal
dc.okm.affiliatedauthorPapageorgiou, Anastassios
dc.okm.affiliatedauthorImran, Mohsin
dc.okm.discipline1182 Biokemia, solu- ja molekyylibiologiafi_FI
dc.okm.discipline1182 Biochemistry, cell and molecular biologyen_GB
dc.okm.internationalcopublicationinternational co-publication
dc.okm.internationalityInternational publication
dc.okm.typeJournal article
dc.publisher.countrySveitsifi_FI
dc.publisher.countrySwitzerlanden_GB
dc.publisher.country-codeCH
dc.relation.articlenumber5962
dc.relation.doi10.3390/ijms20235962
dc.relation.ispartofjournalInternational Journal of Molecular Sciences
dc.relation.issue23
dc.year.issued2019


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