Search results for "Structural Biology."

showing 10 items of 822 documents

GFP immunogold staining, from light to electron microscopy, in mammalian cells.

2012

GFP has emerged as an important reporter for monitoring gene expression, protein localization, cell transformation and cell lineage. The development of GFP as a marker in many different biological systems has emphasized the need to image GFP at high resolution. GFP immunogold labeling with colloidal gold particles becomes essential for electron microscopy (EM) ultrastructural detection. Because of the small size, colloidal gold particles require silver enhancement, a procedure to increase the size of the particle as well as gold toning to stabilize the silver layer. GFP preembedding immunogold staining enables high quality cellular-ultrastructural EM analysis mainly for two reasons, on one …

Staining and LabelingGreen Fluorescent ProteinsGeneral Physics and AstronomyHigh resolutionCell BiologyImmunogold labellingCell lineageBiologyProtein subcellular localization predictionMolecular biologyImmunohistochemistrylaw.inventionGreen fluorescent proteinStructural BiologylawColloidal goldBiophysicsUltrastructureAnimalsHumansGeneral Materials ScienceElectron microscopeFluorescent DyesMicron (Oxford, England : 1993)
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Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis

2008

Staphylococcus aureus alpha-toxin is the archetype of bacterial pore forming toxins and a key virulence factor secreted by the majority of clinical isolates of S. aureus. Toxin monomers bind to target cells and oligomerize to form small beta-barrel pores in the plasma membrane. Many nucleated cells are able to repair a limited number of lesions by unknown, calcium-independent mechanisms. Here we show that cells can internalize alpha-toxin, that uptake is essential for cellular survival, and that pore-complexes are not proteolytically degraded, but returned to the extracellular milieu in the context of exosome-like structures, which we term toxosomes.

Staphylococcus aureusEndosomeBacterial ToxinsBiophysicsEndosomesBiologyEndocytosisHemolysin ProteinsBiochemistryα-ToxinExocytosisVirulence factorExocytosisCell LineHemolysin ProteinsStructural BiologyNucleated cellChlorocebus aethiopsGeneticsExtracellularAnimalsHumansMolecular BiologyCell NucleusBacterial pore forming toxinPore-forming toxinInnate defence mechanismCell BiologyEndocytosisCell biologyExosomeBiochemistryCOS CellsMutationMacrolidesFEBS Letters
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Photothermal nanofibrillar membrane based on hyaluronic acid and graphene oxide to treat Staphylococcus aureus and Pseudomonas aeruginosa infected wo…

2022

Here we reported the fabrication of an electrospun membrane based on a hyaluronic acid derivative (HA-EDA) to be used as a bandage for the potential treatment of chronic wounds. The membrane, loaded with graphene oxide (GO) and ciprofloxacin, showed photothermal properties and light-triggered drug release when irradiated with a near-infrared (NIR) laser beam. Free amino groups of HA-EDA derivative allowed autocrosslinking of the elec- trospun membrane; thus, a substantial enhancement in the hydrolytic resistance of the patch was obtained. In vitro antibacterial activity studies performed on Staphylococcus aureus and Pseudomonas aeruginosa revealed that such electrospun membranes, due to the…

Staphylococcus aureusGeneral MedicineStaphylococcal InfectionsBiochemistryHyaluronan derivative Graphene oxide Nanofibers AntibiofilmAnti-Bacterial AgentsStructural BiologySettore CHIM/09 - Farmaceutico Tecnologico ApplicativoPseudomonas aeruginosaWound InfectionHumansGraphiteHyaluronic AcidMolecular BiologyInternational journal of biological macromolecules
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Detoxication of carcinogenic fjord-region diol epoxides of polycyclic aromatic hydrocarbons by glutathione transferase P1-1 variants and glutathione.

1998

AbstractEpidemiological studies suggest that individuals differing in the expression of allelic variants of the human glutathione transferase (GST) Pi gene differ in susceptibility to chemical carcinogens such as polycyclic aromatic hydrocarbons (PAH). This study reports the catalytic efficiencies (kcat/Km) of two naturally occurring variants, GSTP1-1/I-105 and GSTP1-1/V-105, towards a series of fjord-region diol epoxides representing potent biologically active PAH metabolites, and two GSTP1-1 mutants with Ala105 and Trp105 in the active site. The results indicate that individuals who are homozygous for the allele encoding GSTP1-1/V-105 might be more susceptible to PAH carcinogenesis due to…

StereochemistryCarcinogenesisMutantBiophysicsPolycyclic aromatic hydrocarbonurologic and male genital diseasesBiochemistryCatalysischemistry.chemical_compoundStructure-Activity RelationshipStructural BiologyGeneticspolycyclic compoundsStructure–activity relationshipHumansGlutathione conjugationPolycyclic Aromatic HydrocarbonsMolecular BiologyGeneneoplasmsCarcinogenGlutathione Transferasechemistry.chemical_classificationbiologyMolecular StructureChemistryActive siteGenetic VariationBiological activityCell BiologyGlutathioneGlutathioneFjord regionPolycyclic aromatic hydrocarbonKineticsBiochemistryDiol epoxideHuman glutathione transferase P1-1Inactivation Metabolicbiology.proteinCarcinogensFEBS letters
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The purification and properties of nucleoside phosphotransferase from mucosa of chicken intestine

1984

Abstract (1) Nucleoside phosphotransferase (nucleotide:3′-deoxynucleoside 5′-phosphotransferase, EC 2.7.1.77) has been purified from chicken intestine mucosa to apparent homogeneity. The enzyme is represented by a multisubunit protein at different degrees of association. It can dissociate into a compoenent with a marked fall in catalytic activity. (2) The associated forms are similar to the enzyme previously purified from chick embryo as regards: substrate specificity both with respect to nucleoside monophosphate donors and to deoxyribonucleoside acceptors; sigmoidicity in the rate curve with a variable phosphate donor; instability to heat, dilution and lowering of pH; the activating and pr…

StereochemistryCations DivalentProtein subunitBiophysicsBiologyBiochemistrychemistry.chemical_compoundStructural BiologySettore BIO/10 - BiochimicaNucleoside phosphotransferaseCentrifugation Density GradientAnimalsUreaNucleotideEnzyme kineticsIntestinal MucosaMolecular Biologychemistry.chemical_classificationNucleotidesPhosphotransferasesPhosphatenucleoside phosphotransferaseDeoxyuridineDeoxyribonucleosideMolecular WeightKineticsEnzymechemistryBiochemistryAlcoholsChromatography GelElectrophoresis Polyacrylamide GelChickens
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Crystallization and preliminary X-ray studies of mouse centrin1.

2005

The expression, purification, crystallization and preliminary X-ray diffraction studies of mouse centrin1 are reported. Centrins belong to a family of Ca{sup 2+}-binding EF-hand proteins that play a fundamental role in centrosome duplication and the function of cilia. To shed light on the structure–function relationship of these proteins, mouse centrin1 has been crystallized. The mouse centrin1 has been expressed in Escherichia coli as a GST-centrin fusion protein containing a thrombin protease cleavage site between the fusion partners. Two constructs with different linking-sequence lengths were expressed and purified. Thrombin cleavage yielded functional centrin1 and N-terminally extended …

StereochemistryChromosomal Proteins Non-HistoneMolecular Sequence DataBiophysicsmacromolecular substancesCleavage (embryo)Crystallography X-RayBiochemistrylaw.inventionchemistry.chemical_compoundMiceStructure-Activity RelationshipThrombinStructural BiologylawGeneticsmedicineEscherichia coliAnimalsCentrosome duplicationAmino Acid SequenceCrystallizationDose-Response Relationship DrugCalcium-Binding ProteinsSpace groupCondensed Matter PhysicsFusion proteinRecombinant ProteinsCrystallographyenzymes and coenzymes (carbohydrates)KineticschemistryCrystallization CommunicationsX-ray crystallographybiological scienceshealth occupationsbacteriaCrystallizationEthylene glycolmedicine.drugActa crystallographica. Section F, Structural biology and crystallization communications
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Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina.

2005

Vinorine synthase (VS) is a central enzyme of the biosynthesis of the antiarrhythmic drug ajmaline and is a member of the BAHD superfamily of acyltransferases. So far, no three-dimensional structure with significant sequence homology with VS is known. Crystals of VS and selenomethionyl-labelled VS from the medicinal plant Rauvolfia serpentina have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. VS crystals diffract to 2.8 Å and belong to space group P212121, with unit-cell parameters a = 82.3, b = 89.6, c = 136.2 Å. The selenomethionyl VS crystal was nearly isomorphous with the VS crystal.

StereochemistryCrystallography X-RayRauwolfialaw.inventionIndole AlkaloidsLigaseschemistry.chemical_compoundBiosynthesisStructural BiologylawRauvolfia serpentinamedicineCrystallizationSelenomethioninePlant ProteinsPEG 400chemistry.chemical_classificationATP synthasebiologyGeneral Medicinebiology.organism_classificationAjmalineEnzymechemistryAcyltransferasesbiology.proteinCrystallizationmedicine.drugActa crystallographica. Section D, Biological crystallography
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Eukaryotic tRNAs(Pro): primary structure of the anticodon loop; presence of 5-carbamoylmethyluridine or inosine as the first nucleoside of the antico…

1990

The modified nucleoside U*, located in the first position of the anticodon of yeast, chicken liver and bovine liver tRNA(Pro) (anticodon U*GG), has been determined by means of TLC, HPLC, ultraviolet spectrum and gas chromatography-mass spectrometry. The structure was established as 5-carbamoylmethyluridine (ncm5U). In addition, we report on the primary structures of the above-mentioned tRNAs as well as those which have the IGG anticodon. In yeast, the two tRNA(Pro) (anticodons U*GG and IGG) differ by eight nucleotides, whereas in chicken and in bovine liver, both anticodons are carried by the same 'body tRNA' with one posttranscriptional exception at position 32, where pseudouridine is asso…

StereochemistryMolecular Sequence DataBiophysicsBiologyBiochemistryPseudouridinechemistry.chemical_compoundRNA Transfer ProRNA TransferStructural BiologyYeastsGeneticsmedicineAnticodonAnimalsNucleotideInosineUridinechemistry.chemical_classificationChromatographyBase SequenceMolecular StructureProtein primary structureFungal geneticsRNARNA FungalRNA Transfer Amino Acid-SpecificInosinechemistryBiochemistryTransfer RNANucleic Acid ConformationCattleSpectrophotometry UltravioletNucleosideChickensmedicine.drugBiochimica et biophysica acta
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Coupling of the heme and an internal disulfide bond in human neuroglobin

2004

Neuroglobin displays a hexacoordination His-Fe-His in the absence of external ligands such as oxygen. The observed oxygen affinity therefore depends on the binding rates of both oxygen and the competing distal histidine. Furthermore, the binding properties depend on the presence of an internal disulfide bond. In the case of human neuroglobin, cysteines at positions CD7 and D5 are sufficiently close to form an internal disulfide bond. For cytoglobin, the cysteine residues at positions A7 and GH4 may also form a disulfide bond. Mass spectrometry, ligand binding, and thiol accessibility studies were used to study the role influence of these disulfide bonds. Mutation of specific cysteines, or r…

StereochemistryNeuroglobinGeneral Physics and Astronomychemistry.chemical_elementNerve Tissue ProteinsHemeOxygenMass Spectrometrychemistry.chemical_compoundStructural BiologyHumansGeneral Materials ScienceCysteineDisulfidesHemeHistidinechemistry.chemical_classificationCytoglobinCell BiologyGlobinsOxygenchemistryBiochemistryNeuroglobinThiolOxygen bindingCysteineMicron
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High-resolution crystal structure of an avidin-related protein: insight into high-affinity biotin binding and protein stability.

2004

The chicken avidin gene belongs to an extended gene family encoding seven avidin-related genes (AVRs), of which only avidin is expressed in the chicken. The sequences of AVR4 and AVR5 are identical and the common protein (AVR4) has been expressed both in insect and bacterial systems. The recombinant proteins are similarly hyperthermostable and bind biotin with similarly high affinities. AVR4 was crystallized in the apo and biotin-complexed forms and their structures were determined at high resolution. Its tertiary and quaternary structures are very similar to those of avidin and streptavidin. Its biotin-binding site shows only a few alterations compared with those of avidin and streptavidin…

StreptavidinBiotin bindingHot TemperatureBiotinBiologylaw.inventionchemistry.chemical_compoundBiotinStructural BiologylawAnimalsProtein Structure QuaternaryThermostabilityBacteriaHydrogen BondingGeneral MedicineAvidinAffinitiesBiochemistrychemistryBiotinylationData Interpretation StatisticalBiophysicsRecombinant DNAbiology.proteinStreptavidinCrystallizationBaculoviridaeChickensAvidinProtein BindingActa crystallographica. Section D, Biological crystallography
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