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- W2337690838 abstract "Bacterial ATP-Binding Cassette (ABC) transporters are vital for the uptake of nutrients, including sugars, amino acids, and trace metals. Recent studies have identified two types of importers (Class I and II) based on mechanistic and structural differences. The ribose transporter, RbsABC, is a tripartite ABC importer consisting of a cytoplasmic ABC protein with fused nucleotide-binding domains (NBD), a transmembrane domain (TMD) homodimer, RbsC, and a periplasmic substrate binding protein (SBP), RbsB. However, RbsABC is divergent from canonical importers in the fused ATP-binding cassette, which contains both a consensus and degenerate NBD. This organization is observed in eukaryotic ABC exporters, but is thus far unique among characterized bacterial importers. Despite the asymmetry in the NBDs, significant conformational changes are observed in RbsB during transport based on distance measurements from EPR spectroscopy experiments. These changes are driven by the hydrolysis of ATP, providing a pathway for ribose release from RbsB and subsequent transfer to the cytoplasm. Biochemical and EPR experiments also demonstrate that the association between RbsA and RbsC is sensitive to the availability of nucleotide and stimulates ATP hydrolysis in RbsA, providing tight regulation of the catalytic cycle. Finally, it appears a single consensus ATPase site provides ATP hydrolysis to fuel transport, with rescue mutations failing to restore full activity in the degenerate site. EPR experiments suggest an asymmetric closure of the NBDs in response to magnesium and ATP availability. Whether this proposed opening and closing at a single NBD is sufficient to drive transport of a single ribose molecule is currently unknown. The combined observations suggest RbsABC functions by a mechanism distinct from the well-characterized ABC importers for maltose and vitamin B12. Furthermore, RbsABC may provide a key evolutionary link between bacterial and eukaryotic transporters." @default.
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- W2337690838 date "2016-02-01" @default.
- W2337690838 modified "2023-09-29" @default.
- W2337690838 title "Mechanisms of Bacterial ABC Importers: Lessons from Structural and Functional Studies of the Ribose Transporter" @default.
- W2337690838 doi "https://doi.org/10.1016/j.bpj.2015.11.798" @default.
- W2337690838 hasPublicationYear "2016" @default.
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