ArticleCell research2017
Dimeric structure of the uracil:proton symporter UraA provides mechanistic insights into the SLC4/23/26 transporters.
Article in Cell research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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54 citing papers in PubMed, 112 citations in OpenAlex.
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- Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.Nature communications · 2024Article
- Dimeric transport mechanism of human vitamin C transporter SVCT1.Nature communications · 2024Article
- The role of the STAS domain in SLC26A9 for chloride ion transporter function.Biophysical journal · 2024Article
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- Structural and functional insights into the lipid regulation of human anion exchanger 2.Nature communications · 2024Article
- Mechanism of anion exchange and small-molecule inhibition of pendrin.Nature communications · 2024Article
- Structures and mechanisms of the Arabidopsis cytokinin transporter AZG1.Nature plants · 2024Article
- SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024Review
- Elevator-like movements of prestin mediate outer hair cell electromotility.Nature communications · 2023Article
- Structural insights into the conformational changes of BTR1/SLC4A11 in complex with PIPNature communications · 2023Article
- Insight into the mechanism of HProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter.Nature communications · 2023Article
- Borate Transporters and SLC4 Bicarbonate Transporters Share Key Functional Properties.Membranes · 2023Article
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Authors and funding
13 authors at 6 institutions in 3 countries.
Funding
Abstract
The Escherichia coli uracil:proton symporter UraA is a prototypical member of the nucleobase/ascorbate transporter (NAT) or nucleobase/cation symporter 2 (NCS2) family, which corresponds to the human solute carrier family SLC23. UraA consists of 14 transmembrane segments (TMs) that are organized into two distinct domains, the core domain and the gate domain, a structural fold that is also shared by the SLC4 and SLC26 transporters. Here we present the crystal structure of UraA bound to uracil in an occluded state at 2.5 Å resolution. Structural comparison with the previously reported inward-open UraA reveals pronounced relative motions between the core domain and the gate domain as well as intra-domain rearrangement of the gate domain. The occluded UraA forms a dimer in the structure wherein the gate domains are sandwiched by two core domains. In vitro and in vivo biochemical characterizations show that UraA is at equilibrium between dimer and monomer in all tested detergent micelles, while dimer formation is necessary for the transport activity. Structural comparison between the dimeric UraA and the recently reported inward-facing dimeric UapA provides important insight into the transport mechanism of SLC23 transporters.
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