2021
Structural basis of fast- and slow-severing actin–cofilactin boundaries
Hocky GM, Sindelar CV, Cao W, Voth GA, De La Cruz EM. Structural basis of fast- and slow-severing actin–cofilactin boundaries. Journal Of Biological Chemistry 2021, 296: 100337. PMID: 33508320, PMCID: PMC7961102, DOI: 10.1016/j.jbc.2021.100337.Peer-Reviewed Original Research
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
2013
Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics
Xia S, Wood M, Bradley MJ, De La Cruz EM, Konigsberg WH. Alteration in the cavity size adjacent to the active site of RB69 DNA polymerase changes its conformational dynamics. Nucleic Acids Research 2013, 41: 9077-9089. PMID: 23921641, PMCID: PMC3799440, DOI: 10.1093/nar/gkt674.Peer-Reviewed Original ResearchConceptsRB69 DNA polymeraseFörster resonance energy transferDNA polymeraseHigh-resolution X-ray crystallographyResolution X-ray crystallographyHigh mutation rateB-family polConformational dynamicsExonuclease domainState kinetic parametersMutation rateG mutantResonance energy transferX-ray crystallographyM variantPolymerasePrimer terminusHydrophobic cavityActive siteBase selectivitySimilar substitutionSide chainsProfound effectDramatic effectInternal cavity
2011
Direct Observation of the Myosin Va Recovery Stroke That Contributes to Unidirectional Stepping along Actin
Shiroguchi K, Chin HF, Hannemann DE, Muneyuki E, De La Cruz EM, Kinosita K. Direct Observation of the Myosin Va Recovery Stroke That Contributes to Unidirectional Stepping along Actin. PLOS Biology 2011, 9: e1001031. PMID: 21532738, PMCID: PMC3075224, DOI: 10.1371/journal.pbio.1001031.Peer-Reviewed Original Research
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 systemWidely Distributed Residues in Thymosin β4 Are Critical for Actin Binding
Au JK, Olivares AO, Henn A, Cao W, Safer D, De La Cruz EM. Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding. Biochemistry 2008, 47: 4181-4188. PMID: 18327913, PMCID: PMC2587058, DOI: 10.1021/bi701769u.Peer-Reviewed Original ResearchConceptsActin Binding AffinityActin bindingProline residuesHydrophobic residuesAlanine residuesLysine residuesPro27Thymosin beta4Actin monomersPro29MutagenesisHydrophobic contactsLeu28Slow association rateResiduesLys19Thymosin β4Ile34Tbeta4Lys18Binding affinitiesTwo-step mechanismAssociation ratePro4Cis-trans isomerization
2007
Contributions from All Over
AU JK, DE LA CRUZ EM, SAFER D. Contributions from All Over. Annals Of The New York Academy Of Sciences 2007, 1112: 38-44. PMID: 17468230, DOI: 10.1196/annals.1415.015.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesDrug StabilityKineticsModels, MolecularProtein ConformationRabbitsThermodynamicsThymosinConceptsProline residuesActin bindingWild-type complexHydrophobic contactsSite-directed mutagenesisStrong actin bindingHydrophobic residuesAlanine residuesCysteine 374Slow association rateRate of associationResiduesMutantsComplex variesTbeta4Association rateSulfo-1BindingCis-trans isomerizationKinetic basisComplexesPro27Pro29Lys19Mutagenesis
2006
The Tail Domain of Myosin Va Modulates Actin Binding to One Head
Olivares AO, Chang W, Mooseker MS, Hackney DD, De La Cruz EM. The Tail Domain of Myosin Va Modulates Actin Binding to One Head. Journal Of Biological Chemistry 2006, 281: 31326-31336. PMID: 16921171, DOI: 10.1074/jbc.m603898200.Peer-Reviewed Original Research
2005
Thymosin β4 Induces a Conformational Change in Actin Monomers
Dedova IV, Nikolaeva OP, Safer D, De La Cruz EM, dos Remedios CG. Thymosin β4 Induces a Conformational Change in Actin Monomers. Biophysical Journal 2005, 90: 985-992. PMID: 16272441, PMCID: PMC1367123, DOI: 10.1529/biophysj.105.063081.Peer-Reviewed Original ResearchAcrylamideActinsAdenosine TriphosphateAnimalsCalorimetry, Differential ScanningCysteineElectrophoresis, Polyacrylamide GelFluorescence Resonance Energy TransferHot TemperatureKineticsLysineModels, MolecularMolecular ConformationNucleotidesProtein BindingProtein ConformationProtein Structure, TertiaryPurinesRabbitsSolventsSpectrometry, FluorescenceTemperatureThymosinCofilin Increases the Torsional Flexibility and Dynamics of Actin Filaments
Prochniewicz E, Janson N, Thomas DD, De La Cruz EM. Cofilin Increases the Torsional Flexibility and Dynamics of Actin Filaments. Journal Of Molecular Biology 2005, 353: 990-1000. PMID: 16213521, DOI: 10.1016/j.jmb.2005.09.021.Peer-Reviewed Original Research
2004
Mechanochemical coupling of two substeps in a single myosin V motor
Uemura S, Higuchi H, Olivares AO, De La Cruz EM, Ishiwata S. Mechanochemical coupling of two substeps in a single myosin V motor. Nature Structural & Molecular Biology 2004, 11: 877-883. PMID: 15286720, DOI: 10.1038/nsmb806.Peer-Reviewed Original Research
2002
Actin-induced Closure of the Actin-binding Cleft of Smooth Muscle Myosin*
Yengo CM, De La Cruz EM, Chrin LR, Gaffney DP, Berger CL. Actin-induced Closure of the Actin-binding Cleft of Smooth Muscle Myosin*. Journal Of Biological Chemistry 2002, 277: 24114-24119. PMID: 11959853, DOI: 10.1074/jbc.m111253200.Peer-Reviewed Original Research
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
2000
Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers
De La Cruz E, Ostap E, Brundage R, Reddy K, Sweeney H, Safer D. Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers. Biophysical Journal 2000, 78: 2516-2527. PMID: 10777749, PMCID: PMC1300842, DOI: 10.1016/s0006-3495(00)76797-x.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesBiophysical PhenomenaBiophysicsCircular DichroismCross-Linking ReagentsFluorescent DyesHumansIn Vitro TechniquesKineticsMacromolecular SubstancesModels, MolecularMuscle, SkeletalMutagenesis, Site-DirectedNaphthalenesulfonatesOsmotic PressureProtein BindingProtein ConformationRabbitsRecombinant ProteinsThermodynamicsThymosinTritiumViscosityConceptsActin monomersActin monomer poolMgATP-actinMetazoan cellsNucleotide exchangeC-terminusSubdomain 2Conformational changesMonomer poolN-iodoacetyl-N'Cleavage siteActinThymosin β4Rate of dissociationAmide protonsSulfo-1Unique abilityBindingStructural dynamicsConformationTerminusNucleotidesProteolysisDifferent stabilitiesDegrees CPolymerization and structure of nucleotide-free actin filaments11Edited by W. Baumeister
De La Cruz E, Mandinova A, Steinmetz M, Stoffler D, Aebi U, Pollard T. Polymerization and structure of nucleotide-free actin filaments11Edited by W. Baumeister. Journal Of Molecular Biology 2000, 295: 517-526. PMID: 10623543, DOI: 10.1006/jmbi.1999.3390.Peer-Reviewed Original Research
1995
Nucleotide-free actin: stabilization by sucrose and nucleotide binding kinetics.
De La Cruz EM, Pollard TD. Nucleotide-free actin: stabilization by sucrose and nucleotide binding kinetics. Biochemistry 1995, 34: 5452-61. PMID: 7727403, DOI: 10.1021/bi00016a016.Peer-Reviewed Original Research