2018
14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface
Karlberg T, Hornyak P, Pinto AF, Milanova S, Ebrahimi M, Lindberg M, Püllen N, Nordström A, Löverli E, Caraballo R, Wong EV, Näreoja K, Thorsell AG, Elofsson M, De La Cruz EM, Björkegren C, Schüler H. 14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface. Nature Communications 2018, 9: 3785. PMID: 30224724, PMCID: PMC6141617, DOI: 10.1038/s41467-018-06194-1.Peer-Reviewed Original Research14-3-3 ProteinsADP Ribose TransferasesBacterial ToxinsBinding SitesCrystallography, X-RayEscherichia coliGTPase-Activating ProteinsHost-Pathogen InteractionsHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular ChaperonesProtein ConformationProtein DomainsPseudomonas aeruginosaSaccharomyces cerevisiae
2008
Structural and Energetic Analysis of Activation by a Cyclic Nucleotide Binding Domain
Altieri SL, Clayton GM, Silverman WR, Olivares AO, De La Cruz EM, Thomas LR, Morais-Cabral JH. Structural and Energetic Analysis of Activation by a Cyclic Nucleotide Binding Domain. Journal Of Molecular Biology 2008, 381: 655-669. PMID: 18619611, PMCID: PMC2555981, DOI: 10.1016/j.jmb.2008.06.011.Peer-Reviewed Original ResearchMeSH KeywordsCrystallography, X-RayCyclic AMPCyclic GMPCyclic Nucleotide-Gated Cation ChannelsHydrophobic and Hydrophilic InteractionsModels, MolecularMutationNucleotides, CyclicProtein BindingProtein ConformationProtein Structure, TertiaryConceptsBinding domainsCyclic Nucleotide Binding DomainLigand bindingC-terminal cyclicNucleotide-dependent proteinNucleotide Binding DomainAbsence of ligandFull-length channelLigand-protein interactionsCNB domainsUseful model systemProkaryotic homologResidue side chainsApo stateDependent ion channelsApo configurationsSingle proteinMlotiK1Domain fragmentNucleotide selectivityIon channelsDomain structureX-ray crystallographyX-ray structureModel system