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 tuningFamilyInsectsSubunits
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 simulations