2025
Structural basis of promiscuous inhibition of Listeria virulence activator PrfA by oligopeptides
Hainzl T, Scortti M, Lindgren C, Grundström C, Krypotou E, Vázquez-Boland J, Sauer-Eriksson A. Structural basis of promiscuous inhibition of Listeria virulence activator PrfA by oligopeptides. Cell Reports 2025, 44: 115290. PMID: 39970044, DOI: 10.1016/j.celrep.2025.115290.Peer-Reviewed Original ResearchConceptsDNA-binding helix-turn-helix motifInhibit virulence gene expressionVirulence gene expressionPathogen Listeria monocytogenesPrfA activityVirulence factorsPrfAMaster regulatorsHydrophobic residuesInhibitory bindingGene expressionStructural basisBinding promiscuityPeptide bindingBinding sitesConformational changesPeptide residuesOligopeptidesPeptideInhibitory peptidesBindingPeptide backboneResiduesPromiscuous inhibitionExpression
2015
Origin, diversification and substrate specificity in the family of NCS1/FUR transporters
Krypotou E, Evangelidis T, Bobonis J, Pittis A, GabaldĂłn 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 mechanismsNCS1ProteinResiduesFurDiversificationNidulans
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
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