ArticleNature2009
Structure of a prokaryotic virtual proton pump at 3.2 A resolution.
Article in Nature, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.
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.
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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.
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Who cites it
132 citing papers in PubMed, 226 citations in OpenAlex.
- Structural basis for pH-responsive amino acid transport via SLC7A4.Nature communications · 2026Article
- Structural insights into cationic amino acid transport and viral receptor engagement by CAT1.Nature communications · 2025Article
- Prevalence of oxalotrophy in the human microbiome.BMC genomics · 2025Article
- Examination of conformational dynamics of AdiC transporter with fluorescence-polarization microscopy.The Journal of general physiology · 2025Article
- Structural basis for the substrate recognition and transport mechanism of the human yScience advances · 2025Article
- Cryo-EM structure of the human Asc-1 transporter complex.Nature communications · 2024Article
- The last two transmembrane helices in the APC-type FurE transporter act as an intramolecular chaperone essential for concentrative ER-exit.Microbial cell (Graz, Austria) · 2024Article
- Insights into the Transport Cycle of LAT1 and Interaction with the Inhibitor JPH203.International journal of molecular sciences · 2023Article
- Article
- Integrated AlphaFold2 and DEER investigation of the conformational dynamics of a pH-dependent APC antiporter.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- General principles of secondary active transporter function.Biophysics reviews · 2022Review
- Heteromeric Amino Acid Transporters in Brain: from Physiology to Pathology.Neurochemical research · 2022Review
- Molecular basis for redox control by the human cystine/glutamate antiporter system xcNature communications · 2021Article
- Cation-coupled chloride cotransporters: chemical insights and disease implications.Trends in chemistry · 2021Review
- Article
- Rush Hour of LATs towards Their Transport Cycle.Membranes · 2021Review
- N-terminal Transmembrane-Helix Epitope Tag for X-ray Crystallography and Electron Microscopy of Small Membrane Proteins.Journal of molecular biology · 2021Article
- The Role of the Membrane in Transporter Folding and Activity.Journal of molecular biology · 2021Review
- The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2.Communications biology · 2021Article
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
72 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
To reach the mammalian gut, enteric bacteria must pass through the stomach. Many such organisms survive exposure to the harsh gastric environment (pH 1.5-4) by mounting extreme acid-resistance responses, one of which, the arginine-dependent system of Escherichia coli, has been studied at levels of cellular physiology, molecular genetics and protein biochemistry. This multiprotein system keeps the cytoplasm above pH 5 during acid challenge by continually pumping protons out of the cell using the free energy of arginine decarboxylation. At the heart of the process is a 'virtual proton pump' in the inner membrane, called AdiC, that imports L-arginine from the gastric juice and exports its decarboxylation product agmatine. AdiC belongs to the APC superfamily of membrane proteins, which transports amino acids, polyamines and organic cations in a multitude of biological roles, including delivery of arginine for nitric oxide synthesis, facilitation of insulin release from pancreatic beta-cells, and, when inappropriately overexpressed, provisioning of certain fast-growing neoplastic cells with amino acids. High-resolution structures and detailed transport mechanisms of APC transporters are currently unknown. Here we describe a crystal structure of AdiC at 3.2 A resolution. The protein is captured in an outward-open, substrate-free conformation with transmembrane architecture remarkably similar to that seen in four other families of apparently unrelated transport proteins.
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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.