Featured Publications
Cryo-EM structure of the insect olfactory receptor Orco
Butterwick JA, del Mármol J, Kim KH, Kahlson MA, Rogow JA, Walz T, Ruta V. Cryo-EM structure of the insect olfactory receptor Orco. Nature 2018, 560: 447-452. PMID: 30111839, PMCID: PMC6129982, DOI: 10.1038/s41586-018-0420-8.Peer-Reviewed Original ResearchConceptsAnchor domainOdorant receptorsSingle-particle cryo-electron microscopy structureCryo-electron microscopy structureMinimal sequence conservationReceptor familyRemarkable sequence diversityCryo-EM structureInter-subunit interactionsMicroscopy structureSequence conservationSequence diversityÅ resolutionCentral poreStructural insightsIon channelsOrcoSuch diversityOlfactory systemDiversityEnormous varietyOdor tuningFamilyInsectsSubunitsThe molecular basis of sugar detection by an insect taste receptor
Gomes J, Singh-Bhagania S, Cenci M, Chacon Cordon C, Singh M, Butterwick J. The molecular basis of sugar detection by an insect taste receptor. Nature 2024, 629: 228-234. PMID: 38447670, PMCID: PMC11062906, DOI: 10.1038/s41586-024-07255-w.Peer-Reviewed Original ResearchLigand-binding pocketGustatory receptorsD-fructoseMolecular basisStructure-guided mutagenesisSilkworm Bombyx moriPatterns of chemical groupsIon conductivitySugar selectivityAllosteric pathwaysBombyx moriExperimental binding assaysReceptor-ligand interactionsL-sorboseComputational dockingAromatic residuesActive ligandsAllosteric couplingConformational changesSugar detectionBinding assaysFunctional assaysChemical specificityChemical groupsTaste receptors
2014
Conformational Preferences Underlying Reduced Activity of a Thermophilic Ribonuclease H
Stafford KA, Trbovic N, Butterwick JA, Abel R, Friesner RA, Palmer AG. Conformational Preferences Underlying Reduced Activity of a Thermophilic Ribonuclease H. Journal Of Molecular Biology 2014, 427: 853-866. PMID: 25550198, PMCID: PMC4349505, DOI: 10.1016/j.jmb.2014.11.023.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesCrystallography, X-RayEscherichia coliHot TemperatureHydrophobic and Hydrophilic InteractionsModels, MolecularMolecular Dynamics SimulationMutationNuclear Magnetic Resonance, BiomolecularPrincipal Component AnalysisProtein BindingProtein ConformationRibonuclease HThermodynamicsThermus thermophilusConceptsE. coli homologWild-type proteinRibonuclease HE. coli mutantsGlycine-rich regionMesophilic homologsThermophilus enzymeColi mutantsSubstrate bindingThermophilic proteinsImportant residuesThermus thermophilusConformational dynamicsGlycine residueMesophilic enzymesActive conformationLoop regionAtom MD simulationsConformational basisReduced activityEscherichia coliHomologProteinPosition 80MD simulationsPhosphatidic acid modulation of Kv channel voltage sensor function
Hite RK, Butterwick JA, MacKinnon R. Phosphatidic acid modulation of Kv channel voltage sensor function. ELife 2014, 3: e04366. PMID: 25285449, PMCID: PMC4212207, DOI: 10.7554/elife.04366.Peer-Reviewed Original Research
2010
Solution Structure and Phospholipid Interactions of the Isolated Voltage-Sensor Domain from KvAP
Butterwick JA, MacKinnon R. Solution Structure and Phospholipid Interactions of the Isolated Voltage-Sensor Domain from KvAP. Journal Of Molecular Biology 2010, 403: 591-606. PMID: 20851706, PMCID: PMC2971526, DOI: 10.1016/j.jmb.2010.09.012.Peer-Reviewed Original ResearchConceptsNuclear Overhauser effect spectroscopyNuclear magnetic resonance spectroscopySolution structureIsolated voltage-sensor domainBilayer-forming lipidsMagnetic resonance spectroscopyMicelle interactionsEffect spectroscopyChemical environmentCrystal structurePhospholipid interfaceChemical propertiesResonance spectroscopyPhospholipid micellesMembrane environmentPhospholipid bilayersNanosecond timescaleMillisecond timescaleMicellesSpectroscopyAmphipathic α-helixΑ-helixVoltage sensor domainRelaxation experimentsPhysical properties
2009
Pulsed Electron−Electron Double-Resonance Determination of Spin-Label Distances and Orientations on the Tetrameric Potassium Ion Channel KcsA
Endeward B, Butterwick JA, MacKinnon R, Prisner TF. Pulsed Electron−Electron Double-Resonance Determination of Spin-Label Distances and Orientations on the Tetrameric Potassium Ion Channel KcsA. Journal Of The American Chemical Society 2009, 131: 15246-15250. PMID: 19919160, PMCID: PMC2779547, DOI: 10.1021/ja904808n.Peer-Reviewed Original ResearchConceptsPELDOR dataElectron-electron double resonance measurementsTransverse spin relaxation timeProbe frequencySpin relaxation timeDouble resonance measurementsChannel KcsAMagnetic field strengthSpin-label distancesCentral channel axisPELDOR experimentsDetergent-solubilized samplesField strengthRelaxation timeOscillation frequencyResonance determinationQuantitative simulationChannel axisKcsAFrequencyOrientationMeasurementsAngle
2006
An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H
Butterwick JA, Palmer AG. An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H. Protein Science 2006, 15: 2697-2707. PMID: 17088323, PMCID: PMC2242442, DOI: 10.1110/ps.062398606.Peer-Reviewed Original ResearchConceptsRNase HConformational changesGly residueMesophile Escherichia coliThermophile Thermus thermophilusSolution NMR spectroscopyIntrahelical hydrogen bondsHomologous mesophilicProtein sequencesBiological functionsThermus thermophilusImportant adaptationGly insertionPutative hingeEscherichia coliRibonuclease HMesophilicResiduesDynamic processUnfavorable interactionsThermophilesThermophilicProteinNMR spectroscopyThermophilus
2005
Solution Structure of the Vts1 SAM Domain in the Presence of RNA
Edwards TA, Butterwick JA, Zeng L, Gupta YK, Wang X, Wharton RP, Palmer AG, Aggarwal AK. Solution Structure of the Vts1 SAM Domain in the Presence of RNA. Journal Of Molecular Biology 2005, 356: 1065-1072. PMID: 16405996, DOI: 10.1016/j.jmb.2005.12.004.Peer-Reviewed Original ResearchConceptsSAM domainStructural basisCore helicesMultidimensional heteronuclear NMR spectroscopyRNA-binding surfaceSolution structureChemical shift perturbationsSpecific target RNAHeteronuclear NMR spectroscopyPresence of RNARNA bindingRNA recognitionC-terminusShift perturbationsTarget RNAShort helixMutational dataRNAHelix
2004
Multiple Time Scale Backbone Dynamics of Homologous Thermophilic and Mesophilic Ribonuclease HI Enzymes
Butterwick JA, Loria JP, Astrof NS, Kroenke CD, Cole R, Rance M, Palmer AG. Multiple Time Scale Backbone Dynamics of Homologous Thermophilic and Mesophilic Ribonuclease HI Enzymes. Journal Of Molecular Biology 2004, 339: 855-871. PMID: 15165855, DOI: 10.1016/j.jmb.2004.03.055.Peer-Reviewed Original Research