ArticleBiophysical journal2009
Structural basis of substrate selectivity in the glycerol-3-phosphate: phosphate antiporter GlpT.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- Mechanisms of fosfomycin resistance observed in clinical isolates ofJAC-antimicrobial resistance · 2026Article
- Transport and inhibition of the sphingosine-1-phosphate exporter SPNS2.Nature communications · 2025Article
- A fiducial-assisted strategy compatible with resolving small MFS transporter structures in multiple conformations using cryo-EM.Nature communications · 2025Article
- Molecular insights into substrate translocation in an elevator-type metal transporter.Nature communications · 2024Article
- Molecular insights into substrate translocation in an elevator-type metal transporter.bioRxiv : the preprint server for biology · 2024Article
- Activity of fosfomycin and amikacin against fosfomycin-heteroresistantAntimicrobial agents and chemotherapy · 2023Article
- Fosfomycin resistance mechanisms inFrontiers in cellular and infection microbiology · 2023Review
- Structural basis of ion - substrate coupling in the NaNature communications · 2022Article
- 2-Aminoethylphosphonate utilization in Pseudomonas putida BIRD-1 is controlled by multiple master regulators.Environmental microbiology · 2022Article
- The ups and downs of elevator-type di-/tricarboxylate membrane transporters.The FEBS journal · 2022Article
- Strategies of organic phosphorus recycling by soil bacteria: acquisition, metabolism, and regulation.Environmental microbiology reports · 2022Review
- Membrane Transporters of the Major Facilitator Superfamily Are Essential for Long-Term Maintenance of Phenotypic Tolerance to Multiple Antibiotics in E. coli.Microbiology spectrum · 2021Article
- Transporter characterisation reveals aminoethylphosphonate mineralisation as a key step in the marine phosphorus redox cycle.Nature communications · 2021Article
- Inhibition of the Vesicular Glutamate Transporter (VGLUT) with Congo Red Analogs: New Binding Insights.Neurochemical research · 2021Article
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- Functional Characterization of the Saccharomyces cerevisiae Equilibrative Nucleoside Transporter 1 (ScENT1).Molecules (Basel, Switzerland) · 2018Article
- Insight into determinants of substrate binding and transport in a multidrug efflux protein.Scientific reports · 2016Article
- Atomic-level characterization of transport cycle thermodynamics in the glycerol-3-phosphate:phosphate antiporter.Nature communications · 2015Article
- Yeast Fex1p Is a Constitutively Expressed Fluoride Channel with Functional Asymmetry of Its Two Homologous Domains.The Journal of biological chemistry · 2015Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Major facilitators represent the largest superfamily of secondary active transporter proteins and catalyze the transport of an enormous variety of small solute molecules across biological membranes. However, individual superfamily members, although they may be architecturally similar, exhibit strict specificity toward the substrates they transport. The structural basis of this specificity is poorly understood. A member of the major facilitator superfamily is the glycerol-3-phosphate (G3P) transporter (GlpT) from the Escherichia coli inner membrane. GlpT is an antiporter that transports G3P into the cell in exchange for inorganic phosphate (P(i)). By combining large-scale molecular-dynamics simulations, mutagenesis, substrate-binding affinity, and transport activity assays on GlpT, we were able to identify key amino acid residues that confer substrate specificity upon this protein. Our studies suggest that only a few amino acid residues that line the transporter lumen act as specificity determinants. Whereas R45, K80, H165, and, to a lesser extent Y38, Y42, and Y76 contribute to recognition of both free P(i) and the phosphate moiety of G3P, the residues N162, Y266, and Y393 function in recognition of only the glycerol moiety of G3P. It is the latter interactions that give the transporter a higher affinity to G3P over P(i).
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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.