Idioma:

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

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 D ; Byrne, Bernadette

Nature communications, 2016-04, Vol.7 (1), p.11336-11336, Article 11336 [Periódico revisado por pares]

England: Nature Publishing Group

Texto completo disponível

Citações Citado por

Enviar para

Título:
Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity
Autor: 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 D ; Byrne, Bernadette
Assuntos: Aspergillus nidulans - chemistry ; Aspergillus nidulans - metabolism ; Biological Transport ; Crystallography, X-Ray ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Gene Expression ; Kinetics ; Membrane Transport Proteins - chemistry ; Membrane Transport Proteins - genetics ; Membrane Transport Proteins - metabolism ; Models, Molecular ; Mutation ; Protein Multimerization ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protons ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Substrate Specificity ; Thermodynamics ; Xanthine - chemistry ; Xanthine - metabolism
É parte de: Nature communications, 2016-04, Vol.7 (1), p.11336-11336, Article 11336
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: 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.
Editor: England: Nature Publishing Group
Idioma: Inglês

Links

View this record in MEDLINE/PubMed

Voltar para lista de resultados

Realização: Logos de Redes Sociais:

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

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 D ; Byrne, Bernadette

England: Nature Publishing Group

Buscando em bases de dados remotas. Favor aguardar.