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Structure of eukaryotic purine/H+ symporter UapA suggests a role for homodimerization in transport activity
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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 and Byrne, Bernadette (2016) Structure of eukaryotic purine/H+ symporter UapA suggests a role for homodimerization in transport activity. Nature Communications, 7 . pp. 1-9. 11336. doi:10.1038/ncomms11336 ISSN 2041-1723.
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Official URL: http://dx.doi.org/10.1038/ncomms11336
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-G411VĪ1ā11) 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.
Item Type: | Journal Article | ||||||||
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Subjects: | Q Science > QH Natural history | ||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||||||
Library of Congress Subject Headings (LCSH): | Eukaryotic cells, Biophysics | ||||||||
Journal or Publication Title: | Nature Communications | ||||||||
Publisher: | Nature Publishing Group | ||||||||
ISSN: | 2041-1723 | ||||||||
Official Date: | 18 April 2016 | ||||||||
Dates: |
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Volume: | 7 | ||||||||
Number of Pages: | 9 | ||||||||
Page Range: | pp. 1-9 | ||||||||
Article Number: | 11336 | ||||||||
DOI: | 10.1038/ncomms11336 | ||||||||
Status: | Peer Reviewed | ||||||||
Publication Status: | Published | ||||||||
Access rights to Published version: | Restricted or Subscription Access | ||||||||
Date of first compliant deposit: | 25 April 2016 | ||||||||
Date of first compliant Open Access: | 25 April 2016 | ||||||||
Funder: | Biotechnology and Biological Sciences Research Council (Great Britain) (BBSRC), Seventh Framework Programme (European Commission) (FP7), European Regional Development Fund (ERDF) | ||||||||
Grant number: | BB/K017292/1 (BBSRC), HEALTH-F4-2007- 201924 (FP7) |
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