Search results for "RICH"

showing 10 items of 3360 documents

Topology and accessibility of the transmembrane helices and the sensory site in the bifunctional transporter DcuB of Escherichia coli.

2011

C(4)-Dicarboxylate uptake transporter B (DcuB) of Escherichia coli is a bifunctional transporter that catalyzes fumarate/succinate antiport and serves as a cosensor of the sensor kinase DcuS. Sites and domains of DcuB were analyzed for their topology relative to the cytoplasmic or periplasmic side of the membrane and their accessibility to the water space. For the topology studies, DcuB was fused at 33 sites to the reporter enzymes PhoA and LacZ that are only active when located in the periplasm or the cytoplasm, respectively. The ratios of the PhoA and LacZ activities suggested the presence of 10 or 11 hydrophilic loops, and 11 or 12 α-helical transmembrane domains (TMDs). The central part…

Models MolecularRecombinant Fusion ProteinsMolecular Sequence Datalac operonTopologyBiochemistryProtein Structure SecondaryPolyethylene GlycolsProtein structureBacterial ProteinsCatalytic DomainStilbenesAmino Acid SequenceCysteineBinding sitePeptide sequenceDicarboxylic Acid TransportersEscherichia coli K12ChemistryEscherichia coli ProteinsCell MembranePeriplasmic spaceAlkaline PhosphataseTransmembrane domainMembrane proteinBiochemistryLac OperonEthylmaleimideSulfonic AcidsHydrophobic and Hydrophilic InteractionsCysteineBiochemistry
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Structure-based analyses of Salmonella RcsB variants unravel new features of the Rcs regulon

2021

18 páginas, 7 figuras, 2 tablas

Models MolecularSalmonella typhimuriumIdentificationSignaling SystemTranscription GeneticTranscription FactorAcademicSubjects/SCI00010Protein ConformationProtein Data Bank (RCSB PDB)ExpressionBiologymedicine.disease_causeRegulonBiofilm Formation03 medical and health sciencesBacterial ProteinsCapsule SynthesisStructural BiologyGeneticsmedicineTranscriptional regulationPhosphorylationPromoter Regions GeneticTranscription factorGene030304 developmental biologyRegulation of gene expression0303 health sciencesMutationBinding Sites030306 microbiologyPromoterGene Expression Regulation BacterialBiología y Biomedicina / BiologíaRepressionCell biologyRegulonEscherichia-Coli K-12MutationGenome BacterialPhosphorelay SystemNucleic Acids Research
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Six amino acids define a minimal dimerization sequence and stabilize a transmembrane helix dimer by close packing and hydrogen bonding

2013

AbstractDistinct amino acid sequences have been described to mediate oligomerization of transmembrane α-helices. However, as the sequence context is crucial to determine specificity in transmembrane helix–helix interaction, the question arises how small a sequence can be without losing specificity. In the present analysis, six amino acids have been identified in the PsbF transmembrane helix dimer, which form the contact region of two interacting helices and are directly involved in helix–helix interactions. However, individual amino acids within the complex sequence pattern only together ensure sequence specificity of the analyzed transmembrane helix–helix interactions by mediating close pa…

Models MolecularStereochemistryDimerRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsCytochrome b559Sequence (biology)Context (language use)Cytochrome b559BiologyBiochemistryProtein Structure Secondarychemistry.chemical_compoundBacterial ProteinsStructural BiologyGeneticsEscherichia coliProtein Interaction Domains and MotifsAmino Acid SequenceDimerization motifMolecular Biologychemistry.chemical_classificationSequence contextHydrogen bondProtein StabilityCell MembraneMembrane ProteinsHelix–helix interactionHydrogen BondingCell BiologyCytochrome b GroupTransmembrane proteinTransmembraneAmino acidTransmembrane domainchemistryDimerizationProtein BindingFEBS Letters
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Structural insights into the GTPase domain of Escherichia coli MnmE protein

2007

The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well…

Models MolecularTRNA modificationMagnetic Resonance SpectroscopyGTP'aluminium fluoridehomology modelingMolecular Sequence DataGTPaseGuanosine triphosphateGuanosine DiphosphateBiochemistryeraGTP Phosphohydrolaseschemistry.chemical_compoundStructural BiologyEscherichia coliAmino Acid SequenceHomology modelingBinding siteGTPaseMolecular BiologyBinding SitesSequence Homology Amino AcidChemistryEscherichia coli ProteinsTrmENMRRecombinant ProteinsKineticsBiochemistryMnmEGuanosine diphosphateRap2AGTP PhosphohydrolasesGuanosine TriphosphateSequence AlignmentRasProteins: Structure, Function, and Bioinformatics
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New alkaloid antibiotics that target the DNA topoisomerase I of Streptococcus pneumoniae

2011

16 pags, 3 figs, 3 tabs

Models MolecularTopoisomerase-I Inhibitormedicine.disease_causeMicrobiologyBiochemistryCell LineMicrobiology03 medical and health scienceschemistry.chemical_compoundAlkaloidsBacterial ProteinsStreptococcus pneumoniaemedicineHumansAporphineMolecular BiologyEscherichia coli030304 developmental biologychemistry.chemical_classification0303 health sciencesDose-Response Relationship Drugbiology030306 microbiologyTopoisomeraseCell BiologyPhenanthrenesProtein Structure TertiaryAnti-Bacterial Agents3. Good healthStreptococcus pneumoniaeEnzymeDNA Topoisomerases Type IchemistryBiochemistrybiology.proteinDNA supercoilTopoisomerase I InhibitorsGrowth inhibitionJournal of Biological Chemistry 286: 6402-6413 (2011)
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Enthalpy/entropy compensation effects from cavity desolvation underpin broad ligand binding selectivity for rat odorant binding protein 3

2014

Evolution has produced proteins with exquisite ligand binding specificity, and manipulating this effect has been the basis for much of modern rational drug design. However, there are general classes of proteins with broader ligand selectivity linked to function, the origin of which is poorly understood. The odorant binding proteins (OBPs) sequester volatile molecules for transportation to the olfactory receptors. Rat OBP3, which we characterize by X-ray crystallography and NMR, binds a homologous series of aliphatic gamma-lactones within its aromatic-rich hydrophobic pocket with remarkably little variation in affinity but extensive enthalpy/entropy compensation effects. We show that the bin…

Models Molecular[SDV.BIO]Life Sciences [q-bio]/BiotechnologyOdorant bindingolfactory receptor[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionEnthalpywaterDrug designCrystallography X-RayLigandsReceptors Odorantentropy compensationBiochemistryHydrophobic effectLactonesdifferent chemical classessiteAnimalsMoleculeNuclear Magnetic Resonance Biomolecularisotopically enriched proteinsbiologyChemistrycarbonic-anhydrase[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyLigand (biochemistry)RatsCrystallographyEnthalpy–entropy compensationSolventsOdorant-binding proteinbiology.proteinBiophysicsThermodynamicsidentificationrecognitionsolvent reorganization[SDV.AEN]Life Sciences [q-bio]/Food and NutritionProtein Binding
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Theoretical study of the temperature dependence of dynamic effects in thymidylate synthase.

2010

A theoretical study of the temperature dependence of dynamic effects in the rate limiting step of the reaction catalyzed by thymidylate synthase is presented in this paper. From hybrid Quantum Mechanics/Molecular Mechanics (QM/MM) optimizations of transition state structures within a fully flexible molecular model, free downhill molecular dynamics trajectories have been performed at four different temperatures. The analysis of the reactive and non-reactive trajectories in the enzyme environment has allowed us to study the geometric and electronic coupling between the substrate, the cofactor and the protein. The results show how the contribution of dynamic effects to the rate enhancement mea…

Models MolecularbiologyMolecular modelChemistryHydrideTemperatureGeneral Physics and AstronomySubstrate (chemistry)Active siteThymidylate SynthaseRate-determining stepMolecular mechanicsModels BiologicalMolecular dynamicsKineticsChemical physicsbiology.proteinEscherichia coliPhysical chemistryMoleculePhysical and Theoretical ChemistryPhysical chemistry chemical physics : PCCP
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Effect of tin and lead chlorotriphenyl analogues on selected living cells.

2010

Three kinds of living cells, human embryonic kidney cells, Saccharomyces cerevisiae, and Escherichia coli, were tested for their sensitivity to chlorotriphenyltin and chlorotriphenyllead. The tin compound proved definitely more toxic than the lead derivative, particularly in the case of the human embryonic kidney cells devoid of any protective cell wall. Electron paramagnetic resonance (EPR) comparative studies carried out by using a natural model liposome system (egg yolk lecithin) confirmed considerable changes within the lipid bilayer upon doping by the aforementioned additives, which may be crucial to the mechanism of the observed cell cleavage. The individual dopants revealed diverse i…

Models Molecularfood.ingredientCell SurvivalHealth Toxicology and MutagenesisCellMolecular Conformationchemistry.chemical_elementSaccharomyces cerevisiaeToxicologyCleavage (embryo)BiochemistryLecithinCell wallfoodLecithinsmedicineEscherichia coliOrganometallic CompoundsOrganotin CompoundsHumansChlorotriphenyltinLipid bilayerMolecular BiologyLiposomeElectron Spin Resonance SpectroscopyGeneral MedicineYeastChlorotriphenylleadElectron Paramagnetic Resonancemedicine.anatomical_structureMembraneHEK293 CellsBiochemistrychemistryLeadHuman Embryonic Kidney CellsLiposomesMolecular MedicineTinJournal of biochemical and molecular toxicology
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Effects of temperature and moisture fluctuations on an experimental soil microarthropod community

2001

Summary We established an experiment in microcosms with coniferous forest humus and birch leaf litter for testing the effects of constant vs. diurnally fluctuating temperature and uniform vs. varying moisture, on the population densities and species richness of Collembola and Mestostigmata. These parameters and the vertical distribution of populations were analysed by layers (top, centre, bottom) at two samplings (weeks 10 and 27). The hypotheses were that populations of at least some species benefit from fluctuating microclimate, and that varying conditions permit more species to coexist than uniform conditions. At fluctuating temperature regime, four species and total Collembola were more…

MoistureEcologyMicroclimateSoil ScienceMesostigmataSpecies richnessBiologyPlant litterMicrocosmbiology.organism_classificationPopulation densityEcology Evolution Behavior and SystematicsHumusPedobiologia
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Temporal and spatial fluctuations in moisture affect humus microfungal community structure in microcosms

2000

The effects of temporal and spatial fluctuations in moisture on the microfungal community were studied in birch litter plus pine humus microcosms over 6 months. Two treatments were used: a uniform treatment in which moisture was maintained at the original moisture content throughout the profile over the course of the experiment; and a fluctuating moisture treatment in which the moisture content of the whole microcosm fluctuated weekly around the original moisture content. At 6 months, fungal species richness was higher and diversity was lower under moisture fluctuations than under uniform moisture. The number of fungal isolates and proportional diversity was significantly higher in the bott…

MoistureSoil ScienceSpecies diversityMicrobiologyHumusAgronomyBotanyLitterEnvironmental scienceSpatial variabilitySpecies richnessMicrocosmAgronomy and Crop ScienceWater contentBiology and Fertility of Soils
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