Search results for "Structural Biology."

showing 10 items of 822 documents

The yeast Aft1 transcription factor activates ribonucleotide reductase catalytic subunit RNR1 in response to iron deficiency

2020

Eukaryotic ribonucleotide reductases are iron-dependent enzymes that catalyze the rate-limiting step in the de novo synthesis of deoxyribonucleotides. Multiple mechanisms regulate the activity of ribonucleotide reductases in response to genotoxic stresses and iron deficiency. Upon iron starvation, the Saccharomyces cerevisiae Aft1 transcription factor specifically binds to iron-responsive cis elements within the promoter of a group of genes, known as the iron regulon, activating their transcription. Members of the iron regulon participate in iron acquisition, mobilization and recycling, and trigger a genome-wide metabolic remodeling of iron-dependent pathways. Here, we describe a mechanism …

Transcriptional ActivationRibonucleotideSaccharomyces cerevisiae ProteinsProtein subunitIronSaccharomyces cerevisiaeDeoxyribonucleotidesBiophysicsSaccharomyces cerevisiaeResponse ElementsBiochemistry03 medical and health sciencesStructural BiologyTranscription (biology)Gene Expression Regulation FungalRibonucleotide ReductasesGeneticsMolecular BiologyTranscription factorRibonucleotide reductase030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryIron deficiency030302 biochemistry & molecular biologyHigh Mobility Group ProteinsIron Deficienciesbiology.organism_classificationCell biologyDNA-Binding ProteinsRibonucleotide reductaseRegulonEnzymeYeast/TranscriptionProtein BindingTranscription Factors
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Analyzing Oligomerization of Individual Transmembrane Helices and of Entire Membrane Proteins in E. coli: A Hitchhiker’s Guide to GALLEX

2012

Genetic systems, which allow monitoring interactions of individual transmembrane α-helices within the cytoplasmic membrane of the bacterium Escherichia coli, are now widely used to probe the structural biology and energetics of helix-helix interactions and the consequences of mutations. In contrast to other systems, the GALLEX system allows studying homo- as well as heterooligomerization of individual transmembrane α-helices, and even enables estimation of the energetics of helix-helix interactions within a biological membrane. Given that many polytopic membrane proteins form oligomers within membranes, the GALLEX system represents a unique and powerful approach to monitor formation and sta…

Transmembrane domainMembraneMembrane proteinStructural biologyCytoplasmmedicineBiophysicsBiological membraneBiologyBioinformaticsmedicine.disease_causeEscherichia coliTransmembrane protein
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Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans

2021

AbstractPiwi-interacting RNAs (piRNAs) constitute a class of small RNAs that bind PIWI proteins and are essential to repress transposable elements in the animal germline, thereby promoting genome stability and maintaining fertility. C. elegans piRNAs (21U RNAs) are transcribed individually from minigenes as precursors that require 5’ and 3’ processing. This process depends on the PETISCO complex, consisting of four proteins: IFE-3, TOFU-6, PID-3, and ERH-2. We employ biochemical and structural biology approaches to characterize the PETISCO architecture and its interaction with RNA, together with its effector proteins TOST-1 and PID-1. These two proteins define different PETISCO functions: P…

Transposable elementStructural biologyChemistryEffectorProtein subunitGeneticsPiwi-interacting RNARNABiologyBinding siteBiogenesisDevelopmental BiologyCell biologyGenes & Development
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Interaction of the Alternating Double Stranded Copolymer poly(dA-dT)·poly(dA-dT) with NiCl2and CdCl22: Solution Behavior

2007

The thermal denaturation of the synthetic high molecular weight double stranded polynucleotide poly(dA-dT) x poly(dA-dT) has been studied in aqueous buffered solution (Tris 1.0 mM; pH 7.8+/-0.2) in the presence of increasing concentrations of either Ni(2+) (borderline cation) or Cd(2+) (soft cation) at four different constant ionic strength values (NaCl), making use of UV and circular dichroism (CD) spectroscopies. The experimental results show that the B-type double helix of the polymer is stabilized against thermal denaturation in the presence of both cations at low concentrations, relative to the systems where only NaCl is present, in the same conditions of ionic strength and pH. The eff…

TrisCircular dichroismAqueous solutionChemistryInorganic chemistryGeneral MedicineCrystallographychemistry.chemical_compoundStructural BiologyPolynucleotideIonic strengthHelixCopolymerDenaturation (biochemistry)Molecular BiologyJournal of Biomolecular Structure and Dynamics
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Switch between tyrosinase and catecholoxidase activity of scorpion hemocyanin by allosteric effectors

2008

AbstractPhenoloxidases and hemocyanins have similar type 3 copper centers although they perform different functions. Hemocyanins are oxygen carriers, while phenoloxidases (tyrosinase/catecholoxidase) catalyze the initial step in melanin synthesis. Tyrosinases catalyze two subsequent reactions, whereas catecholoxidases catalyze only the second one. Recent results indicate that hemocyanins can also function as phenoloxidases and here we show for the first time that hemocyanin can be converted to phenoloxidase. Furthermore, its substrate specificity can be switched between catecholoxidase and tyrosinase activity depending on effectors such as hydroxymethyl-aminomethan (Tris) and Mg2+-ions. Thi…

TrisStereochemistrymedicine.medical_treatmentTyrosinaseDopamineAllosteric regulationActivated hemocyaninBiophysicsMagnesium ChlorideTyramineType 3 copper proteinchemical and pharmacologic phenomenaBiochemistryCatalysisSubstrate SpecificityScorpionschemistry.chemical_compoundEnzyme activatorAllosteric RegulationStructural BiologyHemolymphHemolymphGeneticsmedicineAnimalsCatechol oxidaseMolecular BiologyScorpion Pandinus imperatorbiologyMonophenol MonooxygenaseSpectrum AnalysisActive siteCatecholoxidaseHemocyaninCell BiologyEnzyme ActivationchemistryBiochemistryHemocyaninsbiology.proteinTyrosinaseCatechol OxidaseFEBS Letters
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Keyhole Limpet Hemocyanin Type 2 (KLH2): Detection and Immunolocalization of a Labile Functional Unit h

2000

Keyhole limpet hemocyanin (KLH) is a mixture of two hemocyanin isoforms, termed KLH1 and KLH2. Within KLH1 eight oxygen-binding functional units (FUs), 1-a to 1-h, have been identified, in contrast to KLH2, which was previously thought to be organized in seven FUs (2-a to 2-g). By limited proteolysis of KLH2 subunits, isolation of the polypeptide fragments, and N-terminal sequencing, we have now identified an eighth FU of type h, with a molecular mass of 43 kDa. This is unusually small for a FU h from a gastropodan hemocyanin. It is also shown that KLH2 didecamers can be split into a stable and homogeneous population of decamers by dialysis against 50 mM Tris/HCl, pH 7.5, in the absence of …

Trismedicine.medical_treatmentProteolysisMolecular Sequence DataPopulationMegathura crenulataDivalentStructure-Activity Relationshipchemistry.chemical_compoundStructural BiologyEndopeptidasesmedicineAnimalsProtein IsoformsAmino Acid SequenceMicroscopy ImmunoelectronProtein Structure Quaternaryeducationchemistry.chemical_classificationeducation.field_of_studybiologymedicine.diagnostic_testMolecular massAntibodies MonoclonalHemocyaninbiology.organism_classificationMolecular biologyMolecular WeightchemistryMolluscaHemocyaninsbiology.proteinKeyhole limpet hemocyaninJournal of Structural Biology
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Predicting 19F NMR Chemical Shifts: A Combined Computational and Experimental Study of a Trypanosomal Oxidoreductase–Inhibitor Complex

2020

Abstract The absence of fluorine from most biomolecules renders it an excellent probe for NMR spectroscopy to monitor inhibitor–protein interactions. However, predicting the binding mode of a fluorinated ligand from a chemical shift (or vice versa) has been challenging due to the high electron density of the fluorine atom. Nonetheless, reliable 19F chemical‐shift predictions to deduce ligand‐binding modes hold great potential for in silico drug design. Herein, we present a systematic QM/MM study to predict the 19F NMR chemical shifts of a covalently bound fluorinated inhibitor to the essential oxidoreductase tryparedoxin (Tpx) from African trypanosomes, the causative agent of African sleepi…

Trypanosoma brucei bruceiProtozoan ProteinsContext (language use)PyrimidinonesThiophenes010402 general chemistry01 natural sciencesCatalysisquantum chemistryThioredoxinsNMR spectroscopyComputational chemistryOxidoreductasestructural biologyEnzyme InhibitorsNuclear Magnetic Resonance Biomolecularchemistry.chemical_classificationAfrican sleeping sickness010405 organic chemistryChemistryChemical shiftCommunicationGeneral ChemistryNuclear magnetic resonance spectroscopyFluorineOxidoreductase inhibitorLigand (biochemistry)Trypanocidal AgentsCommunications0104 chemical sciencesStructural biologyCovalent bondddc:540Mutationcovalent inhibitorsProtein BindingAngewandte Chemie (International Ed. in English)
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Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine

2005

Strictosidine synthase (STR1) is a central enzyme that participates in the biosynthesis of almost all plant monoterpenoid indole alkaloids. After heterologous expression in Escherichia coli, crystals of STR1 and its substrate complex with tryptamine were obtained by the hanging-drop technique at 302–304 K with potassium sodium tartrate tetrahydrate as precipitant. All crystals belong to space group R3. The native STR1 crystals diffract to 2.95 Å and have unit-cell parameters a = b = 150.3, c = 122.4 Å. The tryptamine complex crystals diffract to 2.38 Å, with unit-cell parameters a = b = 147.3, c = 122.3 Å.

TryptamineStrictosidine synthaseTetrahydratebiologyStereochemistryPotassium sodium tartrateSubstrate (chemistry)General MedicineRauwolfiaTryptamineslaw.inventionchemistry.chemical_compoundchemistryBiosynthesisStructural BiologylawCarbon-Nitrogen Lyasesbiology.proteinHeterologous expressionCrystallizationCrystallizationPlant ProteinsActa Crystallographica Section D Biological Crystallography
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The experimental herbicide UKJ72J is an inhibitor of succinate oxidation in plant mitochondria

1983

not received UKJ72J Herbicide Thiopyrimidine Plant mitochondria Inhibitor Succinate oxidation

UKJ72JInhibitorSuccinate oxidationSaccharomyces cerevisiaeSuccinic AcidBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologySaccharomyces cerevisiaeIn Vitro TechniquesMitochondrionBiochemistry03 medical and health scienceschemistry.chemical_compoundSpecies SpecificityStructural BiologySuccinatesGeneticsAnimalsMolecular BiologyThenoyltrifluoroacetone[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesChromatographybiologyHerbicides030306 microbiologyThiopyrimidinefungifood and beveragesSuccinatesOxidation reductionCell BiologyPlantsbiology.organism_classificationMitochondriaRats3. Good healthAdenosine 5'-triphosphateMOPSPlant mitochondriaPyrimidineschemistryBiochemistrySuccinic acidHerbicideOxidation-Reduction
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UV-induced cross-linking of proteins to plasmid pBR322 containing 8-azidoadenine 2′-deoxyribonucleotides

1988

Abstract An efficient method of cross-linking DNA to protein is described. The method is based on the incorporation of photoactive 8-azidoadenine 2′-deoxyribonucleotides into DNA. We have found that 8-N 3 dATP is a substrate for E. coli DNA polymerase I and that 8-N 3 dATP can be incorporated into plasmid pBR322 by nick-translation. Subsequently we were able to cross-link a set of different proteins to 8-azido-2′-deoxyadenosine-containing pBR322 by UV irradiation (366 nm). No DNA-protein photocross-linking was observed under the same conditions when the non-photoactive plasmid pBR322 was used.

Ultraviolet RaysDNA polymeraseDNA polymerase IIUltraviolet irradiationBiophysicsAzidoadeninePlasmid pBR322BiochemistryHistonesDeoxyadenine NucleotidesPlasmidStructural BiologyEscherichia coliGeneticsNick translationMolecular BiologyPlasmid preparationDNA clampNick-translationbiologyDNA-protein cross-linkCell BiologyDNA Polymerase IPBR322Cross-Linking ReagentsBiochemistrybiology.proteinDNA polymerase IPlasmidsFEBS Letters
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