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Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.


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-G411V?1-11) 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.

SUBMITTER: Alguel Y 

PROVIDER: S-EPMC4837479 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature

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Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.

Alguel Yilmaz Y   Amillis Sotiris S   Leung James J   Lambrinidis George G   Capaldi Stefano S   Scull Nicola J NJ   Craven Gregory G   Iwata So S   Armstrong Alan A   Mikros Emmanuel E   Diallinas George G   Cameron Alexander D AD   Byrne Bernadette B  

Nature communications 20160418


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 re  ...[more]

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