@article {5789,
	title = {Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.},
	journal = {Nat Commun},
	volume = {7},
	year = {2016},
	month = {2016},
	pages = {11336},
	abstract = {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.},
	issn = {2041-1723},
	doi = {10.1038/ncomms11336},
	author = {Alguel, Yilmaz and Amillis, Sotiris and Leung, James and Lambrinidis, George and Capaldi, Stefano and Scull, Nicola J and Craven, Gregory and Iwata, So and Armstrong, Alan and Mikros, Emmanuel and Diallinas, George and Cameron, Alexander D and Byrne, Bernadette}
}
