ArticleThe Journal of biological chemistry2015
In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Characterizing the Conformational Dynamics of the Ribose Transporter B Protein inJournal of chemical theory and computation · 2026Article
- Revisiting strategies to target ABC transporter-mediated drug resistance in CNS cancer.Cancer biology & medicine · 2025Review
- Sulfate-Reducing Bacteria Isolated from an Oil Field in Kazakhstan and a Description ofMicroorganisms · 2024Article
- Identification of crucial roles of transcription factor IhfA on high production of free fatty acids inSynthetic and systems biotechnology · 2024Article
- Exploration of genes encoding KEGG pathway enzymes in rhizospheric microbiome of the wild plant Abutilon fruticosum.AMB Express · 2024Article
- Genomic investigations of diverse corbiculate bee gut-associated Gilliamella reveal conserved pathways for energy metabolism, with diverse and variable energy sources.Access microbiology · 2024Article
- In Silico Analysis of Changes in Predicted Metabolic Capabilities of Intestinal Microbiota after Fecal Microbial Transplantation for Treatment of RecurrentMicroorganisms · 2023Article
- Association between genetic variants of membrane transporters and the risk of high-grade hematologic adverse events in a cohort of Mexican children with B-cell acute lymphoblastic leukemia.Frontiers in oncology · 2023Article
- A methodology for carbamate post-translational modification discovery and its application inInterface focus · 2021Article
- Transporters of glucose and other carbohydrates in bacteria.Pflugers Archiv : European journal of physiology · 2020Review
- The impact of ATP-binding cassette transporters on metabolic diseases.Nutrition & metabolism · 2020Review
- Searching whole genome sequences for biochemical identification features of emerging and reemerging pathogenic Corynebacterium species.Functional & integrative genomics · 2018Article
- Diversity and functions of the sheep faecal microbiota: a multi-omic characterization.Microbial biotechnology · 2017Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
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 Mg(2+). We were able to purify a full complex, RbsABC2, in the presence of stable, transition state mimics (ATP, Mg(2+), and VO4); a RbsAC complex in the presence of ADP and Mg(2+); 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.
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