Search results for "Pheromone binding protein"

showing 5 items of 5 documents

Attracted or repelled?--a matter of two neurons, one pheromone binding protein, and a chiral center.

1998

Abstract Two species of scarab beetles, the Osaka beetle (Anomala osakana) and the Japanese beetle (Popillia japonica), utilize the opposite enantiomers of japonilure, (Z)-5-(1-decenyl)oxacyclopentan-2-one, as their sex pheromones. Each species produces only one of the enantiomers that functions as its own sex pheromone and as a very strong behavioral antagonist for the other species. Using an integrated approach we tested whether the discrimination of these two opposite signals is due to selective filtering by pheromone binding proteins or whether it originates in the specificity of ligand–receptor interactions. We found that the antennae of each of these two scarab species contain only a …

StereochemistryProtein ConformationMolecular Sequence DataBiophysicsBiochemistryPheromonesPopilliaBotanymedicineAnimalsPheromone bindingAmino Acid SequenceCloning MolecularMolecular BiologySensillumNeuronsOlfactory receptorBinding SitesbiologyStereoisomerismCell Biologybiology.organism_classificationChemoreceptor CellsColeopteramedicine.anatomical_structureSex pheromonePheromoneEnantiomerPheromone binding proteinSequence AlignmentSignal TransductionBiochemical and biophysical research communications
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Conformational Change in the Pheromone-binding Protein fromBombyx mori Induced by pH and by Interaction with Membranes

1999

The pheromone-binding protein (PBP) from Bombyx mori was expressed in Escherichia coli periplasm. It specifically bound radiolabeled bombykol, the natural pheromone for this species. It appeared as a single band both in native and SDS-polyacrylamide gel electrophoresis and was also homogeneous in most chromatographic systems. However, in ion-exchange chromatography, multiple forms sometimes appeared. Attempts to separate them revealed that they could be converted into one another. Analysis of the protein by circular dichroism and fluorescence spectroscopy demonstrated that its tertiary structure was sensitive to pH changes and that a dramatic conformational transition occurred between pH 6.…

MaleConformational changeCircular dichroismSensory Receptor CellsProtein ConformationBiochemistryBombykolchemistry.chemical_compoundEscherichia coliAnimalsDenaturation (biochemistry)Pheromone bindingCloning MolecularMolecular BiologyChemistryCircular DichroismCell BiologyHydrogen-Ion ConcentrationBombyxChromatography Ion ExchangeLigand (biochemistry)Protein tertiary structureProtein Structure TertiarySpectrometry FluorescenceBiochemistryBiophysicsInsect ProteinsIntercellular Signaling Peptides and ProteinsThermodynamicsElectrophoresis Polyacrylamide GelCarrier ProteinsPheromone binding proteinJournal of Biological Chemistry
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The crystal structure of a cockroach pheromone-binding protein suggests a new ligand binding and release mechanism.

2003

Pheromone-binding proteins (PBPs) are small helical proteins found in sensorial organs, particularly in the antennae, of moth and other insect species. They were proposed to solubilize and carry the hydrophobic pheromonal compounds through the antennal lymph to receptors, participating thus in the peri-receptor events of signal transduction. The x-ray structure of Bombyx mori PBP (BmorPBP), from male antennae, revealed a six-helix fold forming a cavity that contains the pheromone bombykol. We have identified a PBP (LmaPBP) from the cockroach Leucophaea maderae in the antennae of the females, the gender attracted by pheromones in this species. Here we report the crystal structure of LmaPBP a…

Models MolecularProtein FoldingProtein ConformationMolecular Sequence DataCockroachesCrystallography X-RayLigandsBiochemistryBombykolchemistry.chemical_compoundBombyx moribiology.animalAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyFluorescent DyesCockroachbiologySequence Homology Amino AcidCell BiologyHydrogen-Ion Concentrationbiology.organism_classificationLigand (biochemistry)BombyxButanonesTransport proteinKineticschemistryBiochemistryHelixBiophysicsPheromoneInsect ProteinsFemalePheromone binding proteinCarrier ProteinsProtein BindingThe Journal of biological chemistry
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A pheromone-binding protein from the cockroach Leucophaea maderae: cloning, expression and pheromone binding

2003

0264-6021 (Print) Journal Article; Odorant-binding proteins (OBPs) are thought to transport volatile compounds from air to their receptors through the sensillary lymph. In this protein family, the subgroup of pheromone-binding proteins (PBPs) is specifically tuned to the perception of the sexual pheromone. To date, the description of OBPs has been restricted to Endopterygota and Paraneoptera. Their expression in Orthopteroid has been hypothesized, but no evidence of OBP has been produced in this assemblage to date. In the present study, we describe the first OBP from a Dictyopteran insect that belongs to the cockroach Leucophaea maderae. The PBP of L. maderae (PBPLma) shares all the hallmar…

Carrier Proteins/*genetics/*metabolismProtein familymedia_common.quotation_subjectMolecular Sequence DataCockroachesEndopterygotaInsectBiochemistryPolymerase Chain ReactionPheromonesbiology.animalPheromones/*metabolismAnimalsPheromone bindingAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequenceIn Situ Hybridizationmedia_commonCockroachbiologyBase SequenceMolecularCell Biologybiology.organism_classificationRecombinant ProteinsBiochemistryCockroaches/*physiologyInsect ProteinsPheromoneCarrier ProteinsPheromone binding proteinInsect Proteins/genetics/metabolismRecombinant Proteins/chemistry/metabolismResearch ArticleCloning
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Crystallization and preliminary crystallographic study of a pheromone-binding protein from the cockroachLeucophaea maderae

2002

Pheromone-binding proteins (PBPs) are small helical proteins (13-18 kDa) present in various sensory organs of moths and other insect species. An antennal protein from the cockroach Leucophaea maderae (LmaPBP) has been found to share all the hallmarks of the PBP family and is expressed specifically in the female adult antennae, the gender that perceives the sex pheromone. Here, the crystallization of LmaPBP expressed as a recombinant protein in Escherichia coli periplasm is reported. Crystals of LmaPBP were obtained by the sitting-drop vapour-diffusion method using a nanodrop-dispensing robot. The protein crystallizes in two different crystal forms. Form 1 belongs to space group P1, with uni…

Molecular Sequence DataCockroachesCrystallography X-Raymedicine.disease_causelaw.inventionStructural Biologylawbiology.animalmedicineAnimalsAmino Acid SequenceCrystallizationEscherichia coliCockroachSequence Homology Amino AcidbiologyChemistryResolution (electron density)General MedicinePeriplasmic spaceRecombinant ProteinsCrystallographySex pheromoneRecombinant DNAInsect ProteinsFemaleCarrier ProteinsCrystallizationPheromone binding proteinSequence AlignmentActa Crystallographica Section D Biological Crystallography
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