Imperial College London
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ProfessorBernadetteByrne

Faculty of Natural Sciences, Department of Life Sciences

Associate Dean (Equality, Diversity and Inclusion) for FoNS
 
 
 
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Contact

 

+44 (0)20 7594 3004b.byrne Website

 
 
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Location

 

504Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

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}
}
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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  -
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