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Alguel, Yilmaz; Amillis, Sotiris; Leung, James; Lambrinidis, George; Capaldi, Stefano; Scull, Nicola J.; Craven, Gregory; Iwata, So; Armstrong, Alan; Mikros, Emmanuel; Diallinas, George; Cameron, Alexander; Byrne, Bernadette (2016)
Publisher: Nature Publishing Group
Journal: Nature Communications
Languages: English
Types: Article
Subjects: ACID-XANTHINE PERMEASE, MD Multidisciplinary, SACCHAROMYCES-CEREVISIAE, NAT FAMILY, Multidisciplinary Sciences, ASPERGILLUS-NIDULANS, Article, DOPAMINE TRANSPORTER, CRYSTAL-STRUCTURES, Science & Technology, OLIGOMERIZATION, SEROTONIN TRANSPORTER, QH, REFINEMENT, Science & Technology - Other Topics, MECHANISM
The uric acid/xanthine H+ symporter, UapA, is a high-affinity purine transporter from the filamentous fungus Aspergillus nidulans. Here we present the crystal structure of a genetically stabilized version of UapA (UapA-G411VΔ1–11) in complex with xanthine. UapA is formed from two domains, a core domain and a gate domain, similar to the previously solved uracil transporter UraA, which belongs to the same family. The structure shows UapA in an inward-facing conformation with xanthine bound to residues in the core domain. Unlike UraA, which was observed to be a monomer, UapA forms a dimer in the crystals with dimer interactions formed exclusively through the gate domain. Analysis of dominant negative mutants is consistent with dimerization playing a key role in transport. We postulate that UapA uses an elevator transport mechanism likely to be shared with other structurally homologous transporters including anion exchangers and prestin.\ud

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