ArticleNature communications2014
Structure-based mechanism for Na(+)/melibiose symport by MelB.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.
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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.
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Who cites it
100 citing papers in PubMed, 149 citations in OpenAlex.
- Structure and allostery in major facilitator superfamily symport mechanisms.Acta crystallographica. Section D, Structural biology · 2026Article
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- Structural basis of sodium ion-dependent carnitine transport by OCTN2.Nature communications · 2025Article
- Allosteric effects of the coupling cation in melibiose transporter MelB.bioRxiv : the preprint server for biology · 2025Article
- MFSD2A in Focus: the Molecular Mechanism of Omega-3 Fatty Acid Transport.Physiology (Bethesda, Md.) · 2025Review
- Proteomic Analysis ofFoods (Basel, Switzerland) · 2025Article
- Multiple Pendants-Bearing Triglucosides for Membrane Protein Studies: Effects of Pendant Length and Number on Micelle Interior Hydration and Protein Stability.Biomacromolecules · 2025Article
- Distinct roles of the major binding residues in the cation-binding pocket of MelB.bioRxiv : the preprint server for biology · 2024Article
- Rational Approach to Improve Detergent Efficacy for Membrane Protein Stabilization.Bioconjugate chemistry · 2024Article
- Mobile barrier mechanisms for NaeLife · 2024Article
- Review
- Mobile barrier mechanisms for NabioRxiv : the preprint server for biology · 2023Article
- Melamine-cored glucosides for membrane protein solubilization and stabilization: importance of water-mediated intermolecular hydrogen bonding in detergent performance.Chemical science · 2023Article
- The insertase YidC chaperones the polytopic membrane protein MelB inserting and folding simultaneously from both termini.Structure (London, England : 1993) · 2023Article
- Ins and Outs of Rocker Switch Mechanism in Major Facilitator Superfamily of Transporters.Membranes · 2023Review
- Mfsd2a utilizes a flippase mechanism to mediate omega-3 fatty acid lysolipid transport.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Substrate-binding guides individual melibiose permeases MelB to structurally soften and to destabilize cytoplasmic middle-loop C3.Structure (London, England : 1993) · 2023Article
- Oligomeric state of the aspartate:alanine transporter from Tetragenococcus halophilus.Journal of biochemistry · 2022Article
- Structure and function of HNature communications · 2022Article
- Molecular Basis for the Cation Selectivity of Salmonella typhimurium Melibiose Permease.Journal of molecular biology · 2022Article
40 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The bacterial melibiose permease (MelB) belongs to the glycoside-pentoside-hexuronide:cation symporter family, a part of the major facilitator superfamily (MFS). Structural information regarding glycoside-pentoside-hexuronide:cation symporter family transporters and other Na(+)-coupled permeases within MFS has been lacking, although a wealth of biochemical and biophysical data are available. Here we present the three-dimensional crystal structures of Salmonella typhimurium MelBSt in two conformations, representing an outward partially occluded and an outward inactive state of MelBSt. MelB adopts a typical MFS fold and contains a previously unidentified cation-binding motif. Three conserved acidic residues form a pyramidal-shaped cation-binding site for Na(+), Li(+) or H(+), which is in close proximity to the sugar-binding site. Both cosubstrate-binding sites are mainly contributed by the residues from the amino-terminal domain. These two structures and the functional data presented here provide mechanistic insights into Na(+)/melibiose symport. We also postulate a structural foundation for the conformational cycling necessary for transport catalysed by MFS permeases in general.
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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.