ArticleProceedings of the National Academy of Sciences of the United States of America2013
Structural basis for substrate specificity in the Escherichia coli maltose transport system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed.
- Developing hybrid thiomaltodextrins as specific ligands to the maltodextrin transporter ofRSC advances · 2026Article
- Ligand-binding properties of substrate binding proteins of a maltose uptake system inMicrobiology (Reading, England) · 2026Article
- Molecular mechanism of phosphate import by the bacterial PstSCAB transporter.Nature communications · 2026Article
- A highly conserved ABC transporter mediates cello-oligosaccharide uptake in the extremely thermophilic, lignocellulolytic bacteriumApplied and environmental microbiology · 2026Article
- The Evolution of ABC Importers.Journal of molecular biology · 2025Review
- Maltodextrin transport in the extremely thermophilic, lignocellulose degrading bacteriumJournal of bacteriology · 2025Article
- Synthesis, radiolabeling, and biological evaluation of methyl 6-deoxy-6-[RSC advances · 2025Article
- ATP-binding cassette (ABC) transporters: structures and roles in bacterial pathogenesis.Journal of Zhejiang University. Science. B · 2024Review
- Structural insights into polyamine spermidine uptake by the ABC transporter PotD-PotABC.Science advances · 2024Article
- Expression, purification, and characterization of diacylated Lipo-YcjN frombioRxiv : the preprint server for biology · 2024Article
- How arginine inhibits substrate-binding domain 2 elucidated using molecular dynamics simulations.Protein science : a publication of the Protein Society · 2024Article
- Isothermal titration calorimetry analysis of the binding between the maltodextrin binding protein malE of Staphylococcus aureus with maltodextrins of various lengths.Biochemical and biophysical research communications · 2024Article
- Sugar transport in thermophiles: Bridging lignocellulose deconstruction and bioconversion.Journal of industrial microbiology & biotechnology · 2024Review
- Maltose-Derivatized Fluorescence Turn-On Imaging Probe for Bacteria Detection.ACS infectious diseases · 2023Article
- Binding Specificity of a Novel Cyclo/Maltodextrin-Binding Protein and Its Role in the Cyclodextrin ABC Importer System from Thermoanaerobacterales.Molecules (Basel, Switzerland) · 2023Article
- Fluorinated carbohydrates forChemical Society reviews · 2023Review
- Bactericidal Properties of Proline-RichLife (Basel, Switzerland) · 2022Article
- Programming xenon diffusion in maltose-binding protein.Biophysical journal · 2022Article
- Novel functional insights into a modified sugar-binding protein from Synechococcus MITS9220.Scientific reports · 2022Article
- The C2 entity of chitosugars is crucial in molecular selectivity of the Vibrio campbellii chitoporin.The Journal of biological chemistry · 2021Article
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3 authors.
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Abstract
ATP-binding cassette (ABC) transporters are molecular pumps that harness the chemical energy of ATP hydrolysis to translocate solutes across the membrane. The substrates transported by different ABC transporters are diverse, ranging from small ions to large proteins. Although crystal structures of several ABC transporters are available, a structural basis for substrate recognition is still lacking. For the Escherichia coli maltose transport system, the selectivity of sugar binding to maltose-binding protein (MBP), the periplasmic binding protein, does not fully account for the selectivity of sugar transport. To obtain a molecular understanding of this observation, we determined the crystal structures of the transporter complex MBP-MalFGK2 bound with large malto-oligosaccharide in two different conformational states. In the pretranslocation structure, we found that the transmembrane subunit MalG forms two hydrogen bonds with malto-oligosaccharide at the reducing end. In the outward-facing conformation, the transmembrane subunit MalF binds three glucosyl units from the nonreducing end of the sugar. These structural features explain why modified malto-oligosaccharides are not transported by MalFGK2 despite their high binding affinity to MBP. They also show that in the transport cycle, substrate is channeled from MBP into the transmembrane pathway with a polarity such that both MBP and MalFGK2 contribute to the overall substrate selectivity of the system.
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