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http://purl.uniprot.org/citations/34245266http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34245266http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34245266http://www.w3.org/2000/01/rdf-schema#comment"The polysaccharide lyase family 6 (PL6) represents one of the 41 polysaccharide lyase families classified in the CAZy database with the vast majority of its members being alginate lyases grouped into three subfamilies, PL6_1-3. To decipher the mode of recognition and action of the enzymes belonging to subfamily PL6_1, we solved the crystal structures of Pedsa0632, Patl3640, Pedsa3628 and Pedsa3807, which all show different substrate specificities and mode of action (endo-/exolyase). Thorough exploration of the structures of Pedsa0632 and Patl3640 in complex with their substrates as well as docking experiments confirms that the conserved residues in subsites -1 to +3 of the catalytic site form a common platform that can accommodate various types of alginate in a very similar manner but with a series of original adaptations bringing them their specificities of action. From comparative studies with existing structures of PL6_1 alginate lyases, we observe that in the right-handed parallel β-helix fold shared by all these enzymes, the substrate-binding site harbors the same overall conserved structures and organization. Despite this apparent similarity, it appears that members of the PL6_1 subfamily specifically accommodate and catalyze the degradation of different alginates suggesting that this common platform is actually a highly adaptable and specific tool."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.org/dc/terms/identifier"doi:10.1093/glycob/cwab073"xsd:string
http://purl.uniprot.org/citations/34245266http://purl.org/dc/terms/identifier"doi:10.1093/glycob/cwab073"xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Galisson F."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Galisson F."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Helbert W."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Helbert W."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Aghajari N."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Aghajari N."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Ballut L."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Ballut L."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Carrique L."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Carrique L."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Robert X."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Robert X."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Violot S."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Violot S."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Thureau A."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Thureau A."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Conchou L."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Conchou L."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Jugnarain V."xsd:string
http://purl.uniprot.org/citations/34245266http://purl.uniprot.org/core/author"Jugnarain V."xsd:string