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• W2008410344 abstract "Bacterial ATP-binding cassette (ABC) importers are primary active transporters that are critical for nutrient uptake. Based on structural and functional studies, ABC importers can be divided into two distinct classes, type I and type II. Type I importers follow a strict alternating access mechanism that is driven by the presence of the substrate. Type II importers accept substrates in a nucleotide-free state, with hydrolysis driving an inward facing conformation. The ribose transporter in Escherichia coli is a tripartite complex consisting of a cytoplasmic ATP-binding cassette protein, RbsA, with fused nucleotide binding domains; a transmembrane domain homodimer, RbsC2; and a periplasmic substrate binding protein, RbsB. To investigate the transport mechanism of the complex RbsABC2, we probed intersubunit interactions by varying the presence of the substrate ribose and the hydrolysis cofactors, ATP/ADP and Mg2+. We were able to purify a full complex, RbsABC2, in the presence of stable, transition state mimics (ATP, Mg2+, and VO4); a RbsAC complex in the presence of ADP and Mg2+; and a heretofore unobserved RbsBC complex in the absence of cofactors. The presence of excess ribose also destabilized complex formation between RbsB and RbsC. These observations suggest that RbsABC2 shares functional traits with both type I and type II importers, as well as possessing unique features, and employs a distinct mechanism relative to other ABC transporters.BackgroundThe ribose transporter is a bacterial ABC importer with a non-canonical organization.ResultsThe binding protein complexes with the membrane domain in the absence of substrate, and the ATPase dissociates from the membrane domain during transport.ConclusionA distinct model for transport is proposed from in vitro reassembly conditions and EPR data.SignificanceThe ribose transporter typifies the diversity of ABC transporter mechanisms. Bacterial ATP-binding cassette (ABC) importers are primary active transporters that are critical for nutrient uptake. Based on structural and functional studies, ABC importers can be divided into two distinct classes, type I and type II. Type I importers follow a strict alternating access mechanism that is driven by the presence of the substrate. Type II importers accept substrates in a nucleotide-free state, with hydrolysis driving an inward facing conformation. The ribose transporter in Escherichia coli is a tripartite complex consisting of a cytoplasmic ATP-binding cassette protein, RbsA, with fused nucleotide binding domains; a transmembrane domain homodimer, RbsC2; and a periplasmic substrate binding protein, RbsB. To investigate the transport mechanism of the complex RbsABC2, we probed intersubunit interactions by varying the presence of the substrate ribose and the hydrolysis cofactors, ATP/ADP and Mg2+. We were able to purify a full complex, RbsABC2, in the presence of stable, transition state mimics (ATP, Mg2+, and VO4); a RbsAC complex in the presence of ADP and Mg2+; and a heretofore unobserved RbsBC complex in the absence of cofactors. The presence of excess ribose also destabilized complex formation between RbsB and RbsC. These observations suggest that RbsABC2 shares functional traits with both type I and type II importers, as well as possessing unique features, and employs a distinct mechanism relative to other ABC transporters. The ribose transporter is a bacterial ABC importer with a non-canonical organization. The binding protein complexes with the membrane domain in the absence of substrate, and the ATPase dissociates from the membrane domain during transport. A distinct model for transport is proposed from in vitro reassembly conditions and EPR data." @default.
• W2008410344 created "2016-06-24" @default.
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• W2008410344 date "2015-02-01" @default.
• W2008410344 modified "2023-10-14" @default.
• W2008410344 title "In Vitro Reassembly of the Ribose ATP-binding Cassette Transporter Reveals a Distinct Set of Transport Complexes" @default.
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• W2008410344 doi "https://doi.org/10.1074/jbc.m114.621573" @default.
• W2008410344 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4342470" @default.
• W2008410344 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25533465" @default.
• W2008410344 hasPublicationYear "2015" @default.
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