5I6C

The structure of the eukaryotic purine/H+ symporter, UapA, in complex with Xanthine

5I6C の概要

• エントリーDOI: 10.2210/pdb5i6c/pdb
• 分子名称: Uric acid-xanthine permease, XANTHINE, DODECYL-BETA-D-MALTOSIDE (3 entities in total)
• 機能のキーワード: membrane protein eukaryotic uric acid/xanthine h+ symporter, transport protein
• 由来する生物種: Aspergillus nidulans FGSC A4
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q07307
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 124755.71

構造登録者

Alguel, Y.,Amillis, S.,Leung, J.,Lambrinidis, G.,Capaldi, S.,Scull, N.J.,Craven, G.,Iwata, S.,Armstrong, A.,Mikros, E.,Diallinas, G.,Cameron, A.D.,Byrne, B. (登録日: 2016-02-16, 公開日: 2016-04-27, 最終更新日: 2017-08-30)

主引用文献

Alguel, Y.,Amillis, S.,Leung, J.,Lambrinidis, G.,Capaldi, S.,Scull, N.J.,Craven, G.,Iwata, S.,Armstrong, A.,Mikros, E.,Diallinas, G.,Cameron, A.D.,Byrne, B.
Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.
Nat Commun, 7:11336-11336, 2016

PubMed 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.

PubMed: 27088252
DOI: 10.1038/ncomms11336

実験手法

X-RAY DIFFRACTION (3.7 Å)