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dc.contributor.authorMazurkewich, Scott
dc.contributor.authorHelland, Ronny
dc.contributor.authorMackenzie, Alasdair
dc.contributor.authorEijsink, Vincent
dc.contributor.authorPope, Phillip Byron
dc.contributor.authorBrändén, Gisela
dc.contributor.authorLarsbrink, Johan
dc.date.accessioned2020-11-06T11:49:13Z
dc.date.available2020-11-06T11:49:13Z
dc.date.issued2020-08-13
dc.description.abstractChitin is one of the most abundant renewable organic materials found on earth. The chitin utilization locus in <i>Flavobacterium johnsoniae</i>, which encodes necessary proteins for complete enzymatic depolymerization of crystalline chitin, has recently been characterized but no detailed structural information on the enzymes was provided. Here we present protein structures of the <i>F. johnsoniae</i> chitobiase (<i>Fj</i>GH20) and chitinase B (<i>Fj</i>ChiB). <i>Fj</i>GH20 is a multi-domain enzyme with a helical domain not before observed in other chitobiases and a domain organization reminiscent of GH84 (β-N-acetylglucosaminidase) family members. The structure of <i>Fj</i>ChiB reveals that the protein lacks loops and regions associated with exo-acting activity in other chitinases and instead has a more solvent accessible substrate binding cleft, which is consistent with its <i>endo</i>-chitinase activity. Additionally, small angle X-ray scattering data were collected for the internal 70 kDa region that connects the N- and C-terminal chitinase domains of the unique 158 kDa multi-domain chitinase A (<i>Fj</i>ChiA). The resulting model of the molecular envelope supports bioinformatic predictions of the region comprising six domains, each with similarities to either Fn3-like or Ig-like domains. Taken together, the results provide insights into chitin utilization by <i>F. johnsoniae</i> and reveal structural diversity in bacterial chitin metabolism.en_US
dc.identifier.citationMazurkewich, Helland R, Mackenzie AK, Eijsink V, Pope P, Brändén, Larsbrink J. Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae. Scientific Reports. 2020en_US
dc.identifier.cristinIDFRIDAID 1836628
dc.identifier.doi10.1038/s41598-020-70749-w
dc.identifier.issn2045-2322
dc.identifier.urihttps://hdl.handle.net/10037/19782
dc.language.isoengen_US
dc.publisherNature Researchen_US
dc.relation.journalScientific Reports
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/SYNKNØYT/247732/Norway/Reisestøtte, synkrotron- og nøytronforskning, 2015-2017//en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/BIOTEK2021/221568/Norway/Enzyme development for Norwegian biomass - mining Norwegian biodiversity for seizing Norwegian opportunities in the bio-based economy//en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/RCN/FRIMEDBIO/214042/Norway/The newly discovered Polysaccharide Utilisation Loci linked to multiple cellulolytic systems in nature: how does it work?//en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/EC/MicroDE/336355/Norway/Interpreting the irrecoverable microbiota in digestive ecosystems//en_US
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2020 The Author(s)en_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440en_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440en_US
dc.titleStructural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniaeen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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