Dynamic elements at both cytoplasmically and extracellularly facing sides of the UapA transporter selectively control the accessibility of substrates to their translocation pathway

Journal of Molecular Biology

Volumn 397, Issue 5, 2010, Pages 1132-1143

  Kosti, Vasiliki ^a   Papageorgiou, Ioannis ^a   Diallinas, George ^a  

^a UNIVERSITY OF ATHENS   (Greece)

Author keywords

Aspergillus nidulans; Nucleobase ascorbate transporter (NAT) family; Structure function relationships; Uric acid

Indexed keywords

1 METHYLXANTHINE; 2 THIOXANTHINE; 3 METHYLXANTHINE; ADENINE; GUANINE; HYPOXANTHINE; MUTANT PROTEIN; PERMEASE; PROTEIN UAPA; UNCLASSIFIED DRUG; URACIL; URIC ACID; XANTHINE;

ALLELE; ARTICLE; ASPERGILLUS NIDULANS; CELL GROWTH; CONTROLLED STUDY; ENZYME BINDING; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GENE MUTATION; GENE TRANSLOCATION; MISSENSE MUTATION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN TRANSPORT;

EMERICELLA NIDULANS;

EID: 77950519435     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.02.037     Document Type: Article

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