ArticleNature2012
Structure and mechanism of a glutamate-GABA antiporter.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers, 2 of them syntheses that pooled it.
What it found
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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.
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
104 citing papers in PubMed, 2 syntheses or guidelines pooled it, 200 citations in OpenAlex.
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- Associating mutations causing cystinuria with disease severity with the aim of providing precision medicine.BMC genomics · 2017Pooled it
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- GABA-Producing Bacteria as Potential Psychobiotics in Gut-Brain Axis Regulation.International journal of molecular sciences · 2026Review
- Structural bases of signal generation and transduction by the SPS amino acid sensor of Saccharomyces cerevisiae.G3 (Bethesda, Md.) · 2026Article
- Contrasting effects of glutamate and branched-chain amino acid metabolism on acid tolerance in aApplied and environmental microbiology · 2026Article
- Development and Genomic Evaluation of a Novel Functional Fermented Milk Formulated withFoods (Basel, Switzerland) · 2025Article
- Response and adaptation of verrucomicrobial methanotrophs to heat and acidity.Archives of microbiology · 2025Article
- Structural basis of specific lysine transport by Pseudomonas aeruginosa permease LysP.Nature communications · 2025Article
- EcoFoldDB: Protein Structure-Guided Functional Profiling of Ecologically Relevant Microbial Traits at the Metagenome Scale.Environmental microbiology · 2025Article
- In silico characterization, structural modeling, and molecular docking of GabP in citrus and its potential role in GABA uptake.Scientific reports · 2025Article
- Structural basis for the substrate recognition and transport mechanism of the human yScience advances · 2025Article
- Transport and InsPNature communications · 2025Article
- GlnR positively affects the acid resistance ofFrontiers in microbiology · 2025Article
- Insecticide-Induced Metabolic Dysregulation in Model MicrobeACS omega · 2024Article
- Multitier regulation of theJournal of bacteriology · 2024Article
- Cryo-EM structure of the human Asc-1 transporter complex.Nature communications · 2024Article
- Recent advances in the biosynthesis and industrial biotechnology of Gamma-amino butyric acid.Bioresources and bioprocessing · 2024Review
44 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Food-borne hemorrhagic Escherichia coli, exemplified by the strains O157:H7 and O104:H4 (refs 1, 2), require elaborate acid-resistance systems (ARs) to survive the extremely acidic environment such as the stomach (pH ≈ 2). AR2 expels intracellular protons through the decarboxylation of L-glutamate (Glu) in the cytoplasm and exchange of the reaction product γ-aminobutyric acid (GABA) with extracellular Glu. The latter process is mediated by the Glu-GABA antiporter GadC, a representative member of the amino-acid-polyamine-organocation superfamily of membrane transporters. The functional mechanism of GadC remains largely unknown. Here we show, with the use of an in vitro proteoliposome-based assay, that GadC transports GABA/Glu only under acidic conditions, with no detectable activity at pH values higher than 6.5. We determined the crystal structure of E. coli GadC at 3.1 Å resolution under basic conditions. GadC, comprising 12 transmembrane segments (TMs), exists in a closed state, with its carboxy-terminal domain serving as a plug to block an otherwise inward-open conformation. Structural and biochemical analyses reveal the essential transport residues, identify the transport path and suggest a conserved transport mechanism involving the rigid-body rotation of a helical bundle for GadC and other amino acid antiporters.
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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.