2015
Origin, diversification and substrate specificity in the family of NCS1/FUR transporters
Krypotou E, Evangelidis T, Bobonis J, Pittis A, Gabaldón T, Scazzocchio C, Mikros E, Diallinas G. Origin, diversification and substrate specificity in the family of NCS1/FUR transporters. Molecular Microbiology 2015, 96: 927-950. PMID: 25712422, DOI: 10.1111/mmi.12982.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAspergillus nidulansBinding SitesFungal ProteinsGene DuplicationGene Transfer, HorizontalMembrane Transport ProteinsMolecular Docking SimulationMolecular Dynamics SimulationMutationPhylogenyProtein ConformationProtein Structure, TertiaryPseudogenesSequence Homology, Amino AcidSubstrate SpecificitySymportersConceptsSubstrate specificitySubstrate binding siteFunctional diversificationModel fungus Aspergillus nidulansSystematic mutational analysisBinding sitesStructure-function analysisUptake of purinesNCS1 proteinsPlant homologuesFur proteinAspergillus nidulansGene duplicationHorizontal transferSubstrate dockingMutation analysisSub-familyHomology modelingMolecular mechanismsNCS1ProteinResiduesFurDiversificationNidulansFunctional characterization of NAT/NCS2 proteins of Aspergillus brasiliensis reveals a genuine xanthine–uric acid transporter and an intrinsically misfolded polypeptide
Krypotou E, Scazzocchio C, Diallinas G. Functional characterization of NAT/NCS2 proteins of Aspergillus brasiliensis reveals a genuine xanthine–uric acid transporter and an intrinsically misfolded polypeptide. Fungal Genetics And Biology 2015, 75: 56-63. PMID: 25639910, DOI: 10.1016/j.fgb.2015.01.009.Peer-Reviewed Original ResearchConceptsNucleobase-ascorbate transporterUptake of purinesAcid transportAspergillus nidulansMisfolded polypeptidesER-retainedGFP tagMisfolded proteinsHeterologous expressionEvolutionary implicationsInactive proteinPutative transportersAspergillus brasiliensisFunctional characterizationTurned-overPlasma membranePeptide sequencesIn silicoProteinSubfamilyAspergillusTransport functionLow affinityHigher affinityVacuoles
2014
Modelling, substrate docking and mutational analysis identify residues essential for function and specificity of the major fungal purine transporter AzgA
Krypotou E, Lambrinidis G, Evangelidis T, Mikros E, Diallinas G. Modelling, substrate docking and mutational analysis identify residues essential for function and specificity of the major fungal purine transporter AzgA. Molecular Microbiology 2014, 93: 129-145. PMID: 24818808, DOI: 10.1111/mmi.12646.Peer-Reviewed Original ResearchConceptsSubstrate dockingMutation analysisNucleobase-ascorbate transporterAmino acid residuesNAT familyAspergillus nidulansInverted repeatsSubstrate bindingSubstrate translocationA-helicesPurine bindingC-tailAcid residuesTransporter familyCytoplasmic N-H(+) bindingAzgATMS8TMS10Founding memberFlexible domainsBinding cavityGate domainTMS3Residues