ArticlePloS one2012
Identification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) family.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Nucleobase-ascorbate transporter OsNAT9 regulates seed vigor and drought tolerance by modulating ascorbic acid homeostasis in rice.The Plant journal : for cell and molecular biology · 2025Article
- Insight into the mechanism of HProceedings of the National Academy of Sciences of the United States of America · 2023Article
- L-Ascorbic acid metabolism and regulation in fruit crops.Plant physiology · 2023Article
- Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter.Nature communications · 2023Article
- Exogenous application of xanthine and uric acid and nucleobase-ascorbate transporter MdNAT7 expression regulate salinity tolerance in apple.BMC plant biology · 2021Article
- The solute transport and binding profile of a novel nucleobase cation symporter 2 from the honeybee pathogenFEBS open bio · 2018Article
- Evolution of substrate specificity in the Nucleobase-Ascorbate Transporter (NAT) protein family.Microbial cell (Graz, Austria) · 2018Article
- Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.Biochimica et biophysica acta · 2016Review
- Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.Nature communications · 2016Article
- Targeting the parasite's DNA with methyltriazenyl purine analogs is a safe, selective, and efficacious antitrypanosomal strategy.Antimicrobial agents and chemotherapy · 2015Article
- Sul1 and Sul2 sulfate transceptors signal to protein kinase A upon exit of sulfur starvation.The Journal of biological chemistry · 2015Article
- Molecular dynamics simulations of the bacterial UraA H+-uracil symporter in lipid bilayers reveal a closed state and a selective interaction with cardiolipin.PLoS computational biology · 2015Article
- Modelling and mutational analysis of Aspergillus nidulans UreA, a member of the subfamily of urea/H⁺ transporters in fungi and plants.Open biology · 2014Article
- Understanding transporter specificity and the discrete appearance of channel-like gating domains in transporters.Frontiers in pharmacology · 2014Review
- Functional identification of the hypoxanthine/guanine transporters YjcD and YgfQ and the adenine transporters PurP and YicO of Escherichia coli K-12.The Journal of biological chemistry · 2013Article
- Implications of aberrant temperature-sensitive glucose transport via the glucose transporter deficiency mutant (GLUT1DS) T295M for the alternate-access and fixed-site transport models.The Journal of membrane biology · 2013Article
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5 authors.
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Abstract
Using the crystal structure of the uracil transporter UraA of Escherichia coli, we constructed a 3D model of the Aspergillus nidulans uric acid-xanthine/H(+) symporter UapA, which is a prototype member of the Nucleobase-Ascorbate Transporter (NAT) family. The model consists of 14 transmembrane segments (TMSs) divided into a core and a gate domain, the later being distinctly different from that of UraA. By implementing Molecular Mechanics (MM) simulations and quantitative structure-activity relationship (SAR) approaches, we propose a model for the xanthine-UapA complex where the substrate binding site is formed by the polar side chains of residues E356 (TMS8) and Q408 (TMS10) and the backbones of A407 (TMS10) and F155 (TMS3). In addition, our model shows several polar interactions between TMS1-TMS10, TMS1-TMS3, TMS8-TMS10, which seem critical for UapA transport activity. Using extensive docking calculations we identify a cytoplasm-facing substrate trajectory (D360, A363, G411, T416, R417, V463 and A469) connecting the proposed substrate binding site with the cytoplasm, as well as, a possible outward-facing gate leading towards the substrate major binding site. Most importantly, re-evaluation of the plethora of available and analysis of a number of herein constructed UapA mutations strongly supports the UapA structural model. Furthermore, modeling and docking approaches with mammalian NAT homologues provided a molecular rationale on how specificity in this family of carriers might be determined, and further support the importance of selectivity gates acting independently from the major central substrate binding site.
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