ArticleThe Journal of biological chemistry2014
Insights into the inhibitory mechanisms of the regulatory protein IIA(Glc) on melibiose permease activity.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 32 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
- The molecular mechanism for carbon catabolite repression of the chitin response in Vibrio cholerae.PLoS genetics · 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
- Structures and General Transport Mechanisms by the Major Facilitator Superfamily (MFS).Chemical reviews · 2021Article
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Structural and functional characterization of protein-lipid interactions of the Salmonella typhimurium melibiose transporter MelB.BMC biology · 2018Article
- Regulation of metabolism in Escherichia coli during growth on mixtures of the non-glucose sugars: arabinose, lactose, and xylose.Scientific reports · 2018Article
- Thermodynamic cooperativity of cosubstrate binding and cation selectivity ofThe Journal of general physiology · 2017Article
- Tandem malonate-based glucosides (TMGs) for membrane protein structural studies.Scientific reports · 2017Article
- Thermodynamics of Nanobody Binding to Lactose Permease.Biochemistry · 2016Article
- Insights into Protein-Ligand Interactions: Mechanisms, Models, and Methods.International journal of molecular sciences · 2016Review
- Effect of Detergents on Galactoside Binding by Melibiose Permeases.Biochemistry · 2015Article
- Thermodynamic mechanism for inhibition of lactose permease by the phosphotransferase protein IIAGlc.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The phosphotransfer protein IIA(Glc) of the bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system plays a key role in the regulation of carbohydrate metabolism. Melibiose permease (MelB) is one among several permeases subject to IIA(Glc) regulation. The regulatory mechanisms are poorly understood; in addition, thermodynamic features of IIA(Glc) binding to other proteins are also unknown. Applying isothermal titration calorimetry and amine-specific cross-linking, we show that IIA(Glc) directly binds to MelB of Salmonella typhimurium (MelB(St)) and Escherichia coli MelB (MelB(Ec)) at a stoichiometry of unity in the absence or presence of melibiose. The dissociation constant values are 3-10 μM for MelB(St) and 25 μM for MelB(Ec). All of the binding is solely driven by favorable enthalpy forces. IIA(Glc) binding to MelB(St) in the absence or presence of melibiose yields a large negative heat capacity change; in addition, the conformational entropy is constrained upon the binding. We further found that the IIA(Glc)-bound MelB(St) exhibits a decreased binding affinity for melibiose or nitrophenyl-α-galactoside. It is believed that sugar binding to the permease is involved in an induced fit mechanism, and the transport process requires conformational cycling between different states. Thus, the thermodynamic data are consistent with the interpretation that IIA(Glc) inhibits the induced fit process and restricts the conformational dynamics of MelB(St).
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.