Search results for "bacteri"

showing 10 items of 5466 documents

Crystal structure of the N-terminal domain of the major virulence factor BB0323 from the Lyme disease agent Borrelia burgdorferi.

2019

Lyme disease is an infection caused by the spirochete Borrelia burgdorferi after it is transmitted to a mammalian organism during a tick blood meal. B. burgdorferi encodes at least 140 lipoproteins located on the outer or inner membrane, thus facing the surroundings or the periplasmic space, respectively. However, most of the predicted lipoproteins are of unknown function, and only a few proteins are known to be essential for the persistence and virulence of the pathogen. One such protein is the periplasmic BB0323, which is indispensable for B. burgdorferi to cause Lyme disease and the function of which is associated with cell fission and outer membrane integrity. After expression and trans…

Models MolecularLyme DiseaseVirulence FactorsLipoproteinsVirulencePeriplasmic spaceBiologybiology.organism_classificationVirulence factorCell biologyBacterial ProteinsStructural BiologyBorrelia burgdorferiInner membraneSpectrinAmino Acid SequenceBorrelia burgdorferiBacterial outer membranePathogenActa crystallographica. Section D, Structural biology
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Backbone dynamics of rusticyanin: the high hydrophobicity and rigidity of this blue copper protein is responsible for its thermodynamic properties.

2003

Local dynamics and solute-solvent exchange properties of rusticyanin (Rc) from Thiobacillus ferrooxidans have been studied by applying heteronuclear ((1)H, (15)N) NMR spectroscopy. (15)N relaxation parameters have been determined for the reduced protein, and a model-free analysis has been applied. The high average value of the generalized order parameter, S(2) (0.93), indicates that Rc is very rigid. The analysis of cross correlation rates recorded in both the reduced and the oxidized forms conclusively proves that Rc possesses the same dynamic features in both oxidation states. The accessibility of backbone amide protons to the solvent at different time scales has also been studied by appl…

Models MolecularMagnetic Resonance SpectroscopyCopper proteinWaterNuclear magnetic resonance spectroscopyThiobacillusBiochemistryProtein Structure SecondaryProtein Structure TertiarySolventMetalchemistry.chemical_compoundCrystallographyProtein structureHeteronuclear moleculechemistryBacterial ProteinsAzurinvisual_artAmideRusticyaninvisual_art.visual_art_mediumThermodynamicsHydrophobic and Hydrophilic InteractionsCopperBiochemistry
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The Nature of the Stimulus and of the Fumarate Binding Site of the Fumarate Sensor DcuS of Escherichia coli

2005

DcuS is a membrane-associated sensory histidine kinase of Escherichia coli specific for C(4) -dicarboxylates. The nature of the stimulus and its structural prerequisites were determined by measuring the induction of DcuS-dependent dcuB'-'lacZ gene expression. C(4)-dicarboxylates without or with substitutions at C2/C3 by hydrophilic (hydroxy, amino, or thiolate) groups stimulated gene expression in a similar way. When one carboxylate was replaced by sulfonate, methoxy, or nitro groups, only the latter (3-nitropropionate) was active. Thus, the ligand of DcuS has to carry two carboxylate or carboxylate/nitro groups 3.1-3.8 A apart from each other. The effector concentrations for half-maximal i…

Models MolecularMagnetic Resonance SpectroscopyHistidine KinaseRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeBiochemistryCitric AcidStructure-Activity Relationshipchemistry.chemical_compoundFumaratesEscherichia colimedicineDicarboxylic AcidsAmino Acid SequenceCarboxylatePhosphorylationBinding siteKinase activityTartratesMolecular BiologyEscherichia coliPeptide sequenceDicarboxylic Acid TransportersBinding SitesChemistryEscherichia coli ProteinsAutophosphorylationHistidine kinaseGene Expression Regulation BacterialCell BiologyNitro CompoundsPeptide FragmentsEnzyme ActivationLac OperonBiochemistryMutagenesis Site-DirectedPropionatesProtein KinasesSequence AlignmentBinding domainJournal of Biological Chemistry
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(Trifluoromethoxy)Phenylboronic Acids: Structures, Properties, and Antibacterial Activity.

2021

Three isomers of (trifluoromethoxy)phenylboronic acids were studied in the context of their physicochemical, structural, antimicrobial and spectroscopic properties. They were characterized by 1H, 13C, 11B and 19F NMR spectroscopy. The acidity of all the isomers was evaluated by both spectrophotometric and potentiometric titrations. The introduction of the -OCF3 group influences the acidity, depending, however, on the position of a substituent, with the ortho isomer being the least acidic. Molecular and crystal structures of ortho and para isomers were determined by the single crystal XRD method. Hydrogen bonded dimers are the basic structural motives of the investigated molecules in the sol…

Models MolecularMagnetic Resonance SpectroscopyPotentiometric titrationSubstituentMolecular ConformationPharmaceutical ScienceContext (language use)Crystal structureMicrobial Sensitivity TestsDFTMedicinal chemistryArticleOCF<sub>3</sub>Analytical Chemistrylcsh:QD241-441chemistry.chemical_compoundlcsh:Organic chemistryDrug StabilityIsomerismtrifluoromethoxyDrug DiscoveryMoleculePhysical and Theoretical ChemistryMolecular StructureHydrogen bondOrganic ChemistryBoronic AcidsNMRAnti-Bacterial AgentsantibacterialchemistryChemistry (miscellaneous)Intramolecular forceX-RayMolecular MedicineisomersOCF3Derivative (chemistry)Molecules (Basel, Switzerland)
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Stereoselective synthesis of the published structure of feigrisolide A. Structural revision of feigrisolides A and B.

2006

The total synthesis of the proposed structure of feigrisolide A is reported. Ethyl (S)-3-hydroxybutyrate was the chiral starting material. A Brown asymmetric allylation and an Evans aldol reaction were key steps of the synthesis. The NMR data of the synthetic product are different from those of the natural product. The published structure of feigrisolide A is therefore erroneous. A subsequent comparison of spectral data strongly suggests that feigrisolides A and B are identical with (-)-nonactic acid and (+)-homononactic acid, respectively.

Models MolecularMagnetic Resonance SpectroscopyStereochemistryMolecular ConformationStereoisomerismChemical synthesischemistry.chemical_compoundLactonesStructure-Activity RelationshipAldol reactionSpectral dataNatural productMolecular StructureChemistryorganic chemicalsOrganic ChemistryEnantioselective synthesisTotal synthesisStereoisomerismGeneral MedicineNuclear magnetic resonance spectroscopyNmr dataAnti-Bacterial AgentsProduct (mathematics)Aldol condensationStereoselectivityThe Journal of organic chemistry
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Polyketide Derivatives from Mangrove Derived Endophytic Fungus Pseudopestalotiopsis theae

2020

Chemical investigation of secondary metabolites from the endophytic fungus Pseudopestalotiopsis theae led to the isolation of eighteen new polyketide derivatives, pestalotheols I&ndash

Models MolecularMagnetic Resonance SpectroscopyStereochemistryPharmaceutical Science010402 general chemistry01 natural sciencesArticlePolyketidepolyketideDrug DiscoverymedicineEndophytesCytotoxicityPharmacology Toxicology and Pharmaceutics (miscellaneous)IC50lcsh:QH301-705.5endophytic fungusbiologyMolecular Structure010405 organic chemistryChemistryAbsolute configurationFungibiology.organism_classification0104 chemical sciencesAcinetobacter baumanniiPseudopestalotiopsis theaelcsh:Biology (General)<i>Pseudopestalotiopsis theae</i>PolyketidesFermentationColistincytotoxicityRhizophoraceaeAntibacterial activityTwo-dimensional nuclear magnetic resonance spectroscopymedicine.drugMarine Drugs
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Site-specific Labelling with a Metal Chelator for Protein-structure Refinement

2004

A single free Cys sidechain in the N-terminal domain of the E. coli arginine repressor was covalently derivatized with S-cysteaminyl-EDTA for site-specific attachment of paramagnetic metal ions. The effects of chelated metal ions were monitored with (15)N-HSQC spectra. Complexation of Co(2+), which has a fast relaxing electron spin, resulted in significant pseudocontact shifts, but also in peak doubling which was attributed to the possibility of forming two different stereoisomers of the EDTA-Co(2+) complex. In contrast, complexation of Cu(2+) or Mn(2+), which have slowly relaxing electron spins, did not produce chemical shift changes and yielded self-consistent sets of paramagnetic relaxat…

Models MolecularMagnetic Resonance SpectroscopyTime FactorsMetal ions in aqueous solutionElectronsGadoliniumBiochemistryIonParamagnetismchemistry.chemical_compoundNuclear magnetic resonanceBacterial ProteinsAmideEscherichia coliChelationCysteineEdetic AcidSpectroscopyChelating AgentsIonsManganeseElectronic correlationChemistryRelaxation (NMR)Electron Spin Resonance SpectroscopyProteinsCobaltDNAProtein Structure TertiaryRepressor ProteinsCrystallographyModels ChemicalCovalent bondProtonsCopperJournal of Biomolecular NMR
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Atomic Mean-Square Displacements in Proteins by Molecular Dynamics: A Case for Analysis of Variance

2004

AbstractInformation on protein internal motions is usually obtained through the analysis of atomic mean-square displacements, which are a measure of variability of the atomic positions distribution functions. We report a statistical approach to analyze molecular dynamics data on these displacements that is based on probability distribution functions. Using a technique inspired by the analysis of variance, we compute unbiased, reliable mean-square displacements of the atoms and analyze them statistically. We applied this procedure to characterize protein thermostability by comparing the results for a thermophilic enzyme and a mesophilic homolog. In agreement with previous experimental observ…

Models MolecularMean squareSurface (mathematics)Hot TemperatureTime FactorsNitrogenProtein ConformationMolecular ConformationBiophysicsBiophysical Theory and ModelingMeasure (mathematics)Protein Structure SecondaryMolecular dynamicsBacterial ProteinsStatistical physicsProbabilityThermostabilityAnalysis of VarianceQuantitative Biology::BiomoleculesModels StatisticalChemistryProteinsModels TheoreticalCrystallographyDistribution functionSolventsProbability distributionAnalysis of varianceAlgorithms
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Peptides Derived from Apoptotic Bax and Bid Reproduce the Poration Activity of the Parent Full-Length Proteins

2005

Bax and Bid are proapoptotic proteins of the Bcl-2 family that regulate the release of apoptogenic factors from mitochondria. Although they localize constitutively in the cytoplasm, their apoptotic function is exerted at the mitochondrial outer membrane, and is related to their ability to form transbilayer pores. Here we report the poration activity of fragments from these two proteins, containing the first alpha-helix of a colicinlike hydrophobic hairpin (alpha-helix 5 of Bax and alpha-helix 6 of Bid). Both peptides readily bind to synthetic lipid vesicles, where they adopt predominantly alpha-helical structures and induce the release of entrapped calcein. In planar lipid membranes they fo…

Models MolecularMolecular Sequence DataBiophysicsApoptosisPeptideIn Vitro TechniquesBiophysical PhenomenaIon ChannelsPermeabilityProtein Structure Secondarychemistry.chemical_compoundBcl-2-associated X proteinSpectroscopy Fourier Transform InfraredHumansChannels Receptors and Electrical SignalingAmino Acid SequencePeptide sequenceIon channelbcl-2-Associated X Proteinchemistry.chemical_classificationbiologyChemistryCircular DichroismPeptide FragmentsCell biologyCalceinMembraneProto-Oncogene Proteins c-bcl-2CytoplasmMultiprotein ComplexesLiposomesbiology.proteinPèptidsCarrier ProteinsBacterial outer membraneProteïnesBH3 Interacting Domain Death Agonist ProteinBiophysical Journal
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Crystal structure of the infectious phenotype-associated outer surface protein BBA66 from the Lyme disease agent Borrelia burgdorferi

2014

Borrelia burgdorferi, the causative agent of Lyme disease is transmitted to the mammalian host organisms by infected Ixodes ticks. Transfer of the spirochaetal bacteria from Ixodes ticks to the warm-blooded mammalian organism provides a challenge for the bacteria to adapt and survive in the different environmental conditions. B. burgdorferi has managed to differentially express genes in response to the encountered changes such as temperature and pH variance or metabolic rate to survive in both environments. In recent years, much interest has been turned on genes that are upregulated during the borrelial transfer to mammalian organisms as this could reveal the proteins important in the patho…

Models MolecularMolecular Sequence DataSequence alignmentCrystallography X-RayMicrobiologyMicrobiologyLyme diseasemedicineAnimalsAmino Acid SequenceBorrelia burgdorferiGeneAntigens BacterialLyme DiseaseIxodesbiologyProtein superfamilybiology.organism_classificationmedicine.diseasePhenotypeInfectious DiseasesMembrane proteinBorrelia burgdorferiInsect ScienceParasitologyIxodesSequence AlignmentBacterial Outer Membrane ProteinsTicks and Tick-borne Diseases
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