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Ribose import binding protein RbsB is a periplasmic protein found in Gram-negative bacteria, such as Escherichia coli and Brucella melitensis, where it serves as a high-affinity receptor for D-ribose [1, 22]. It belongs to the periplasmic binding protein (PBP) superfamily and functions through a 'Venus flytrap' mechanism, undergoing a significant conformational change from an open to a closed state upon ligand binding [8, 16]. This closed form interacts with the RbsABC ATP-binding cassette (ABC) transporter complex to facilitate the uptake of ribose into the cytoplasm and with the Trg chemoreceptor to mediate positive chemotaxis [1, 5, 8]. Beyond its metabolic roles, RbsB is involved in quorum sensing by interacting with autoinducer-2 (AI-2) and plays a role in modulating bacterial conjugation and biofilm formation [18, 23, 25]. Although it is not currently a target for FDA-approved drugs, its essential role in bacterial fitness, virulence, and environmental sensing makes it a promising candidate for the development of novel antimicrobial strategies and highly specific biosensors [7, 11, 22].
Ligand binding induces a conformational change (Venus flytrap mechanism) that allows the protein to interact with the RbsABC transporter complex for ribose import or with chemoreceptors like Trg for chemotaxis [1, 5, 8, 16].
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