ArticleThe Journal of biological chemistry2008
Projection structure of a member of the amino acid/polyamine/organocation transporter superfamily.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- Article
- Article
- Article
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- Insights into the Structure, Function, and Ligand Discovery of the Large Neutral Amino Acid Transporter 1, LAT1.International journal of molecular sciences · 2018Review
- Effects of Mutations and Ligands on the Thermostability of the l-Arginine/Agmatine Antiporter AdiC and Deduced Insights into Ligand-Binding of Human l-Type Amino Acid Transporters.International journal of molecular sciences · 2018Article
- Insights into the molecular basis for substrate binding and specificity of the wild-type L-arginine/agmatine antiporter AdiC.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Substrate selectivity of the acid-activated glutamate/γ-aminobutyric acid (GABA) antiporter GadC from Escherichia coli.The Journal of biological chemistry · 2013Article
- A pipeline for comprehensive and automated processing of electron diffraction data in IPLT.Journal of structural biology · 2013Article
- Measuring substrate binding and affinity of purified membrane transport proteins using the scintillation proximity assay.Nature protocols · 2012Article
- Protonation of glutamate 208 induces the release of agmatine in an outward-facing conformation of an arginine/agmatine antiporter.The Journal of biological chemistry · 2011Article
- Molecular basis of substrate-induced permeation by an amino acid antiporter.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Role of transmembrane domain 8 in substrate selectivity and translocation of SteT, a member of the L-amino acid transporter (LAT) family.The Journal of biological chemistry · 2010Article
- Article
- A conserved Na(+) binding site of the sodium-coupled neutral amino acid transporter 2 (SNAT2).The Journal of biological chemistry · 2009Article
- Structure and mechanism of a Na+-independent amino acid transporter.Science (New York, N.Y.) · 2009Article
- Article
- Substrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
10 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The L-arginine/agmatine antiporter AdiC is a key component of the arginine-dependent extreme acid resistance system of Escherichia coli. Phylogenetic analysis indicated that AdiC belongs to the amino acid/polyamine/organocation (APC) transporter superfamily having sequence identities of 15-17% to eukaryotic and human APC transporters. For functional and structural characterization, we cloned, overexpressed, and purified wild-type AdiC and the point mutant AdiC-W293L, which is unable to bind and consequently transport L-arginine. Purified detergent-solubilized AdiC particles were dimeric. Reconstitution experiments yielded two-dimensional crystals of AdiC-W293L diffracting beyond 6 angstroms resolution from which we determined the projection structure at 6.5 angstroms resolution. The projection map showed 10-12 density peaks per monomer and suggested mainly tilted helices with the exception of one distinct perpendicular membrane spanning alpha-helix. Comparison of AdiC-W293L with the projection map of the oxalate/formate antiporter from Oxalobacter formigenes, a member from the major facilitator superfamily, indicated different structures. Thus, two-dimensional crystals of AdiC-W293L yielded the first detailed view of a transport protein from the APC superfamily at sub-nanometer resolution.
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