ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structural insights into the activation mechanism of melibiose permease by sodium binding.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 50 citations in OpenAlex.
- Structure and allostery in major facilitator superfamily symport mechanisms.Acta crystallographica. Section D, Structural biology · 2026Article
- Article
- Allosteric effects of the coupling cation in melibiose transporter MelB.bioRxiv : the preprint server for biology · 2025Article
- Distinct roles of the major binding residues in the cation-binding pocket of MelB.bioRxiv : the preprint server for biology · 2024Article
- Mobile barrier mechanisms for NaeLife · 2024Article
- Mobile barrier mechanisms for NabioRxiv : the preprint server for biology · 2023Article
- Substrate-binding guides individual melibiose permeases MelB to structurally soften and to destabilize cytoplasmic middle-loop C3.Structure (London, England : 1993) · 2023Article
- Molecular Basis for the Cation Selectivity of Salmonella typhimurium Melibiose Permease.Journal of molecular biology · 2022Article
- Cooperative binding ensures the obligatory melibiose/Na+ cotransport in MelB.The Journal of general physiology · 2021Article
- X-ray crystallography reveals molecular recognition mechanism for sugar binding in a melibiose transporter MelB.Communications biology · 2021Article
- Article
- Structural biology workflow for the expression and characterization of functional human sodium glucose transporter type 1 in Pichia pastoris.Scientific reports · 2019Article
- Structural properties determining low KThe Journal of biological chemistry · 2018Article
- Thermodynamic cooperativity of cosubstrate binding and cation selectivity ofThe Journal of general physiology · 2017Article
- Helical unwinding and side-chain unlocking unravel the outward open conformation of the melibiose transporter.Scientific reports · 2016Article
- Effect of Detergents on Galactoside Binding by Melibiose Permeases.Biochemistry · 2015Article
- The Melibiose Transporter of Escherichia coli: CRITICAL CONTRIBUTION OF LYS-377 TO THE STRUCTURAL ORGANIZATION OF THE INTERACTING SUBSTRATE BINDING SITES.The Journal of biological chemistry · 2015Article
- Insights into the inhibitory mechanisms of the regulatory protein IIA(Glc) on melibiose permease activity.The Journal of biological chemistry · 2014Article
- Suppression of conformation-compromised mutants of Salmonella enterica serovar Typhimurium MelB.Journal of bacteriology · 2014Article
- Proton transfer and protein conformation dynamics in photosensitive proteins by time-resolved step-scan Fourier-transform infrared spectroscopy.Journal of visualized experiments : JoVE · 2014Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The melibiose carrier from Escherichia coli (MelB) couples the accumulation of the disaccharide melibiose to the downhill entry of H(+), Na(+), or Li(+). In this work, substrate-induced FTIR difference spectroscopy was used in combination with fluorescence spectroscopy to quantitatively compare the conformational properties of MelB mutants, implicated previously in sodium binding, with those of a fully functional Cys-less MelB permease. The results first suggest that Asp55 and Asp59 are essential ligands for Na(+) binding. Secondly, though Asp124 is not essential for Na(+) binding, this acidic residue may play a critical role, possibly by its interaction with the bound cation, in the full Na(+)-induced conformational changes required for efficient coupling between the ion- and sugar-binding sites; this residue may also be a sugar ligand. Thirdly, Asp19 does not participate in Na(+) binding but it is a melibiose ligand. The location of these residues in two independent threading models of MelB is consistent with their proposed role.
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