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
2011
Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate
Wu X, Bradley MJ, Cai Y, Kümmel D, De La Cruz EM, Barr FA, Reinisch KM. Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 18672-18677. PMID: 22065758, PMCID: PMC3219131, DOI: 10.1073/pnas.1110415108.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBiological TransportCrystallography, X-RayDeath Domain Receptor Signaling Adaptor ProteinsGuanineGuanine Nucleotide Exchange FactorsHumansKineticsNucleotidesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRab GTP-Binding ProteinsRab1 GTP-Binding ProteinsConceptsGuanine nucleotide exchange factorsDENN domain proteinsMembrane traffic pathwaysNucleotide exchange factorsGDP-bound formGTP-bound formSwitch regions IHigher eukaryotesRab GTPasesGEF familyEukaryotic cellsTraffic pathwaysExchange factorSwitch INucleotide bindingKey regulatorConformational changesFirst structureNovel insightsRab35ProteinDENND1BEukaryotesRegion IGTPases
2010
Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11
Kucera K, Koblansky AA, Saunders LP, Frederick KB, De La Cruz EM, Ghosh S, Modis Y. Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11. Journal Of Molecular Biology 2010, 403: 616-629. PMID: 20851125, PMCID: PMC2957522, DOI: 10.1016/j.jmb.2010.09.022.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceCrystallography, X-RayDNA PrimersImmunity, InnateIn Vitro TechniquesMacrophages, PeritonealMiceMice, KnockoutModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsPlasmodium falciparumProfilinsProtein Structure, SecondaryProtozoan ProteinsRabbitsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionStatic ElectricityToll-Like ReceptorsToxoplasmaConceptsAcidic loopToll-like receptor 11Β-hairpinLong β-hairpinApicomplexan parasite Cryptosporidium parvumActin-binding surfaceFilament barbed endsStructure-based analysisYeast profilinGondii profilinProfilin mutantsGliding motilityParasite Cryptosporidium parvumT. gondii profilinNucleotide exchangeToxoplasma gondii profilinRabbit actinPlasmodium falciparum resultsActin polymerizationApicomplexan protozoaHomologous loopBarbed endsHost cellsIL-12 secretionInnate immune response
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 ResearchConceptsBinding 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
2007
Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c‐myc inhibition
Crichlow GV, Zhou H, Hsiao HH, Frederick KB, Debrosse M, Yang Y, Folta-Stogniew EJ, Chung HJ, Fan C, De La Cruz EM, Levens D, Lolis E, Braddock D. Dimerization of FIR upon FUSE DNA binding suggests a mechanism of c‐myc inhibition. The EMBO Journal 2007, 27: 277-289. PMID: 18059478, PMCID: PMC2206118, DOI: 10.1038/sj.emboj.7601936.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCrystallography, X-RayDimerizationDNADNA HelicasesDNA-Binding ProteinsDrosophila ProteinsGene Expression RegulationHumansMagnetic Resonance SpectroscopyMolecular Sequence DataPromoter Regions, GeneticProtein BindingProto-Oncogene Proteins c-mycRepressor ProteinsRNA Splicing FactorsRNA-Binding ProteinsTranscription Factor TFIIHConceptsRRM domainDNA bindingFirst RRM domainSecond RRM domainC-myc transcriptional controlSite-directed mutationsDNA upstreamTranscriptional controlInfluences transcriptionC-Myc inhibitionNucleic acid recognitionPromoter sitesP1 promoterAnalogous mutationCell homeostasisC-MycTFIIHProteinLight scattering revealBinding sitesDNATranscriptionSingle strandsMutationsSize exclusion chromatography
2001
Structural biology. Actin' up.
De La Cruz E, Pollard T. Structural biology. Actin' up. Science 2001, 293: 616-8. PMID: 11474090, DOI: 10.1126/science.1063558.Peer-Reviewed Original ResearchActin Depolymerizing FactorsActinsAdenosine DiphosphateAdenosine TriphosphateBiopolymersContractile ProteinsCrystallography, X-RayHydrolysisMicrofilament ProteinsPhosphatesProfilinsProtein BindingProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsRhodaminesThymosin