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dc.contributor.authorDe Santi, Concetta
dc.contributor.authorGani, Osman A. B. S. M.
dc.contributor.authorHelland, Ronny
dc.contributor.authorWilliamson, Adele Kim
dc.date.accessioned2018-03-26T09:00:49Z
dc.date.available2018-03-26T09:00:49Z
dc.date.issued2017-12-08
dc.description.abstractThe 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.en_US
dc.descriptionSource at <a href=http://dx.doi.org/10.1038/s41598-017-17677-4> http://dx.doi.org/10.1038/s41598-017-17677-4 </a>.en_US
dc.identifier.citationDe Santi, C., Gani, O. A., Helland, R., Williamson, A. K. (2017) Structural insight into a CE15 esterase from the marine bacterial metagenome. Scientific Reports. 7:17278:1-10en_US
dc.identifier.cristinIDFRIDAID 1573106
dc.identifier.doi10.1038/s41598-017-17677-4
dc.identifier.issn2045-2322
dc.identifier.urihttps://hdl.handle.net/10037/12439
dc.language.isoengen_US
dc.publisherNature Publishing Groupen_US
dc.relation.journalScientific Reports
dc.rights.accessRightsopenAccessen_US
dc.subjectEnzyme mechanismsen_US
dc.subjectX-ray crystallographyen_US
dc.subjectVDP::Matematikk og Naturvitenskap: 400::Kjemi: 440en_US
dc.subjectVDP::Mathematics and natural science: 400::Chemistry: 440en_US
dc.titleStructural insight into a CE15 esterase from the marine bacterial metagenomeen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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