BibTex format
@article{Byrne:2016:10.1038/ncomms11336,
author = {Byrne, B and Alguel, Y and Scull, NJ and Craven, G and Armstrong, A and Iwata, S and Diallinas, G and Amillis, S and Capaldi, S and Cameron, AD and Lambrinidis, G and Mikros, E},
doi = {10.1038/ncomms11336},
journal = {Nature Communications},
pages = {1--9},
title = {Structure of eukaryotic purine/Hþ symporter UapA suggests a role for homodimerization in transport activity},
url = {http://dx.doi.org/10.1038/ncomms11336},
volume = {7},
year = {2016}
}
RIS format (EndNote, RefMan)
TY - JOUR
AB - 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.
AU - Byrne,B
AU - Alguel,Y
AU - Scull,NJ
AU - Craven,G
AU - Armstrong,A
AU - Iwata,S
AU - Diallinas,G
AU - Amillis,S
AU - Capaldi,S
AU - Cameron,AD
AU - Lambrinidis,G
AU - Mikros,E
DO - 10.1038/ncomms11336
EP - 9
PY - 2016///
SN - 2041-1723
SP - 1
TI - Structure of eukaryotic purine/Hþ symporter UapA suggests a role for homodimerization in transport activity
T2 - Nature Communications
UR - http://dx.doi.org/10.1038/ncomms11336
UR - https://www.nature.com/articles/ncomms11336
UR - http://hdl.handle.net/10044/1/29775
VL - 7
ER -
