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
2012
Modeling, Substrate Docking, and Mutational Analysis Identify Residues Essential for the Function and Specificity of a Eukaryotic Purine-Cytosine NCS1 Transporter*
Krypotou E, Kosti V, Amillis S, Myrianthopoulos V, Mikros E, Diallinas G. Modeling, Substrate Docking, and Mutational Analysis Identify Residues Essential for the Function and Specificity of a Eukaryotic Purine-Cytosine NCS1 Transporter*. Journal Of Biological Chemistry 2012, 287: 36792-36803. PMID: 22969088, PMCID: PMC3481282, DOI: 10.1074/jbc.m112.400382.Peer-Reviewed Original ResearchMeSH KeywordsAdenineAmino Acid MotifsAmino Acid SubstitutionAspergillus nidulansConserved SequenceCytosineFungal ProteinsGuanineHydrogen BondingHypoxanthineKineticsMolecular Docking SimulationMolecular Dynamics SimulationMutagenesis, Site-DirectedPhenotypeProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidStructural Homology, ProteinSubstrate SpecificitySymportersConceptsAsn-350Substrate binding siteAsn-163Substrate bindingSubstrate dockingSer-85Trp-259Substrate binding residuesPrimary sequence alignmentBinding sitesSubstrate binding affinitySystematic functional analysisTransmembrane a-helicesEukaryotic membersSequence alignmentBacterial membersA-helicesCritical residuesC-tailMicrobacterium liquefaciensRelevant mutantsCytoplasmic N-Binding residuesTMS1TMS6
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply