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http://purl.uniprot.org/citations/32325255http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32325255http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32325255http://www.w3.org/2000/01/rdf-schema#comment"The endo-β-1,4-mannanase from the hyperthermostable bacterium Thermotoga petrophila (TpMan) is an enzyme that catalyzes the hydrolysis of mannan and heteromannan polysaccharides. Of the three domains that comprise TpMan, the N-terminal GH5 catalytic domain and the C-terminal carbohydrate-binding domain are connected through a central ancillary domain of unknown structure and function. In this study, we report the partial crystal structure of the TpMan at 1.45 Å resolution, so far, the first modular hyperthermostable endo-β-1,4-mannanase structure determined. The structure exhibits two domains, a (β/α)8-barrel GH5 catalytic domain connected via a linker to the central domain with an immunoglobulin-like β-sandwich fold formed of seven β-strands. Functional analysis showed that whereas the immunoglobulin-like domain does not have the carbohydrate-binding function, it stacks on the GH5 catalytic domain acting as a thermostabilizing domain and allowing operation at hyperthermophilic conditions. The carbohydrate-binding domain is absent in the crystal structure most likely due to its high flexibility around the immunoglobulin-like domain which may act also as a pivot. These results represent new structural and functional information useful on biotechnological applications for biofuel and food industries."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.org/dc/terms/identifier"doi:10.1016/j.bbapap.2020.140437"xsd:string
http://purl.uniprot.org/citations/32325255http://purl.org/dc/terms/identifier"doi:10.1016/j.bbapap.2020.140437"xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Nicolet Y."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Nicolet Y."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Martin L."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Martin L."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Squina F.M."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Squina F.M."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Speranca M.A."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Speranca M.A."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Garcia W."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Garcia W."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Muniz J.R.C."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Muniz J.R.C."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Cabral A.D."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"Cabral A.D."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"da Silva V.M."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/author"da Silva V.M."xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/name"Biochim Biophys Acta Proteins Proteom"xsd:string
http://purl.uniprot.org/citations/32325255http://purl.uniprot.org/core/name"Biochim Biophys Acta Proteins Proteom"xsd:string