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http://purl.uniprot.org/citations/26235029http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26235029http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26235029http://www.w3.org/2000/01/rdf-schema#comment"The acidic polysaccharide alginate represents a promising marine biomass for the microbial production of biofuels, although the molecular and structural characteristics of alginate transporters remain to be clarified. In Sphingomonas sp. A1, the ATP-binding cassette transporter AlgM1M2SS is responsible for the import of alginate across the cytoplasmic membrane. Here, we present the substrate-transport characteristics and quaternary structure of AlgM1M2SS. The addition of poly- or oligoalginate enhanced the ATPase activity of reconstituted AlgM1M2SS coupled with one of the periplasmic solute-binding proteins, AlgQ1 or AlgQ2. External fluorescence-labeled oligoalginates were specifically imported into AlgM1M2SS-containing proteoliposomes in the presence of AlgQ2, ATP, and Mg(2+). The crystal structure of AlgQ2-bound AlgM1M2SS adopts an inward-facing conformation. The interaction between AlgQ2 and AlgM1M2SS induces the formation of an alginate-binding tunnel-like structure accessible to the solvent. The translocation route inside the transmembrane domains contains charged residues suitable for the import of acidic saccharides."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2015.06.021"xsd:string
http://purl.uniprot.org/citations/26235029http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2015.06.021"xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Itoh T."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Itoh T."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Mikami B."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Mikami B."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Maruyama Y."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Maruyama Y."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Nishitani Y."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Nishitani Y."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Murata K."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Murata K."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Kaneko A."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Kaneko A."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Hashimoto W."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/author"Hashimoto W."xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/date"2015"xsd:gYear
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/pages"1643-1654"xsd:string
http://purl.uniprot.org/citations/26235029http://purl.uniprot.org/core/pages"1643-1654"xsd:string