Search results for "Streptomyce"

showing 10 items of 103 documents

An enantioselective synthesis of the C(33)–C(37) fragment of Amphotericin B

2003

An enantioselective synthesis of the C(33)–C(37) tripropionate fragment of Amphotericin B has been developed in only 6 steps. Peer reviewed

Models MolecularAntifungal Agentsnatural productsFragment (computer graphics)ChemistryStereochemistryasymmetric synthesisOrganic ChemistryEnantioselective synthesisEstersStereoisomerismLigandsBiochemistryStreptomycesorganic chemistryModels ChemicalAmphotericin BAmphotericin BmedicinePhysical and Theoretical Chemistrymedicine.drugOrg. Biomol. Chem.
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Cholesterol oxidase: ultrahigh-resolution crystal structure and multipolar atom model-based analysis

2015

International audience; Author(s) of this paper may load this reprint on their own web site or institutional repository provided that this cover page is retained. Republication of this article or its storage in electronic databases other than as specified above is not permitted without prior permission in writing from the IUCr. For further information see http://journals.iucr.org/services/authorrights.html Acta Cryst. (2015). D71, 954-968 Zarychta et al. · Cholesterol oxidase research papers 954 http://dx. Examination of protein structure at the subatomic level is required to improve the understanding of enzymatic function. For this purpose, X-ray diffraction data have been collected at 100…

Models MolecularElectron densityCholesterol oxidaseProtein ConformationCrystallography X-Ray010402 general chemistry01 natural sciences03 medical and health scienceschemistry.chemical_compoundProtein structureStructural Biologycholesterol oxidase[CHIM.CRIS]Chemical Sciences/Cristallography[CHIM]Chemical Sciences030304 developmental biologyFlavin adenine dinucleotide0303 health sciencesHydrogen bondIntermolecular forceResolution (electron density)Hydrogen BondingGeneral MedicineStreptomyces0104 chemical sciencesBond lengthCrystallographychemistryFlavin-Adenine Dinucleotide
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The First Crystal Structure of Tyrosinase: All Questions Answered?

2006

Models MolecularProtein FoldingBinding SitesbiologyMonophenol MonooxygenaseProtein ConformationChemistryStereochemistryTyrosinaseBioinorganic chemistryGeneral ChemistryPlasma protein bindingGeneral MedicineCrystal structurebiology.organism_classificationCrystallography X-RayStreptomycesCatalysisStreptomycesProtein structureBiochemistryProtein foldingBinding siteProtein BindingChemInform
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Abyssomicin E, a highly functionalized polycyclic metabolite from Streptomyces species.

2007

Abyssomicin E (1), a new polycyclic metabolite with a C19 skeleton, was isolated from Streptomyces sp. (HKI0381). Its chemical structure was determined by comprehensive NMR and MS spectroscopic analyses. For the first time in this recently discovered class of compounds, the absolute stereochemistry was directly established by subsequent single-crystal X-ray diffraction study using anomalous dispersion with copper radiation.

Models MolecularbiologyMolecular StructureChemistryStereochemistryChemical structureMetaboliteOrganic ChemistryGeneral MedicineAbyssomicin Ebiology.organism_classificationBridged Bicyclo Compounds HeterocyclicBiochemistryStreptomycesStreptomyces speciesStreptomyceschemistry.chemical_compoundOrganic chemistryPhysical and Theoretical ChemistryOrganic letters
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Unravelling the DNA sequences carried by Streptomyces coelicolor membrane vesicles

2022

AbstractMembrane vesicles (MVs) are spherical particles with nanoscale dimensions and characterized by the presence of diverse cargos, such as nucleic acids, proteins, lipids, and cellular metabolites. Many examples of (micro)organisms producing MVs are reported in literature. Among them, bacterial MVs are of particular interest because they are now considered as the fourth mechanism of horizontal gene transfer. Streptomyces bacteria are well-known for their ecological roles and ability to synthesize bioactive compounds, with Streptomyces coelicolor being the model organism. It was previously demonstrated that it can produce distinct populations of MVs characterized by different protein and…

MultidisciplinaryBacteriaBacterial ProteinsBase SequenceNucleic AcidsRNAStreptomyces coelicolorGene Expression Regulation BacterialSettore BIO/19 - Microbiologia GeneraleLipids
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Efficacy of natamycin for control of growth and ochratoxin A production by Aspergillus carbonarius strains under different environmental conditions

2007

Aims:  To examine the efficacy of natamycin produced by Streptomyces natalensis against strains of Aspergillus carbonarius growth and ochratoxin A (OTA) production under different environmental factors on a grape juice-based medium. Methods and Results:  Detailed studies in the range 0–20 ng ml−1 for control of growth and ochratoxin production by strains of A. carbonarius at 0·98, 0·96 and 0·94 water availabilities (aw) and 15–25°C on a fresh red grape extract medium were examined. Inhibition of growth was depending on temperature and aw level. At 15°C, 5–10 ng ml−1 natamycin was effective in reducing growth almost completely. However, at 20–25°C and all the three aw levels, growth was only…

Ochratoxin AAspergillusPreservativebiologyMohoGeneral Medicinebiology.organism_classificationApplied Microbiology and BiotechnologyMicrobiologychemistry.chemical_compoundNatamycinchemistrymedicineFood microbiologyFood scienceStreptomyces natalensisOchratoxinBiotechnologymedicine.drugJournal of Applied Microbiology
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The Streptomyces coelicolor dnaK operon contains a second promoter driving the expression of the negative regulator hspR at physiological temperature

2006

HspR (heat shock protein regulator) acts as a negative regulator of different genes in many bacteria. In Streptomyces coelicolor hspR gene is part and the transcriptional repressor of the dnaK operon which encodes the DnaK, GrpE, DnaJ chaperone machines and HspR itself. Our experiments led us to the discovery of a second promoter, internal to dnaK operon, located upstream hspR gene. Transcription from this promoter was detected at 30 degrees C indicating that hspR could play a key physiological role.

OperonMolecular Sequence Datagenetic processesRegulatorStreptomyces coelicolorBiochemistryMicrobiologyheat shock responseBacterial ProteinsTranscription (biology)Heat shock proteinOperonGeneticsHSP70 Heat-Shock ProteinsHeat shockPromoter Regions GeneticMolecular BiologyGeneHeat-Shock ProteinsGeneticsBase SequencebiologyReverse Transcriptase Polymerase Chain ReactionStreptomyces coelicolorTemperatureGene Expression Regulation BacterialGeneral Medicinebiology.organism_classificationRepressor ProteinshspRChaperone (protein)biological sciencesbiology.proteinbacteriaArchives of Microbiology
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Broad Spectrum Thiopeptide Recognition Specificity of theStreptomyces lividans TipAL Protein and Its Role in Regulating Gene Expression

1999

Microbial metabolites isolated in screening programs for their ability to activate transcription of the tipA promoter (ptipA) in Streptomyces lividans define a class of cyclic thiopeptide antibiotics having dehydroalanine side chains ("tails"). Here we show that such compounds of heterogeneous primary structure (representatives tested: thiostrepton, nosiheptide, berninamycin, promothiocin) are all recognized by TipAS and TipAL, two in-frame translation products of the tipA gene. The N-terminal helix-turn-helix DNA binding motif of TipAL is homologous to the MerR family of transcriptional activators, while the C terminus forms a novel ligand-binding domain. ptipA inducers formed irreversible…

Protein ConformationMolecular Sequence DataMutantBiologyBiochemistryStreptomycesMass SpectrometryThiostreptonchemistry.chemical_compoundProtein structureBacterial ProteinsDehydroalanineAmino Acid SequenceMolecular BiologyRegulation of gene expressionAlanineProtein primary structureGene Expression Regulation BacterialCell Biologybiology.organism_classificationStreptomycesAnti-Bacterial AgentschemistryBiochemistryTrans-ActivatorsPeptidesNosiheptideJournal of Biological Chemistry
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Proteomics highlights metabolic changes associated with n-hexadecane utilization in a Streptomyces coelicolor engineered strain.

2011

Proteomics n-hexadecane utilization Streptomyces coelicolor genetically engineered strain.
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TrpM, a Small Protein Modulating Tryptophan Biosynthesis and Morpho-Physiological Differentiation in Streptomyces coelicolor A3(2).

2016

In the model actinomycete Streptomyces coelicolor A3(2), small open reading frames encoding proteins with unknown functions were identified in several amino acid biosynthetic gene operons, such as SCO2038 (trpX) in the tryptophan trpCXBA locus. In this study, the role of the corresponding protein in tryptophan biosynthesis was investigated by combining phenotypic and molecular analyses. The 2038KO mutant strain was characterized by delayed growth, smaller aerial hyphae and reduced production of spores and actinorhodin antibiotic, with respect to the WT strain. The capability of this mutant to grow on minimal medium was rescued by tryptophan and tryptophan precursor (serine and/or indole) su…

Proteomics0301 basic medicineProtein ExtractionMutantlcsh:MedicineStreptomyces coelicolor A3(2)Settore BIO/19 - Microbiologia GeneraleBiochemistrySerinechemistry.chemical_compoundAromatic Amino AcidsSmall ProteinAntibioticsTRPMMicrobial PhysiologyMedicine and Health SciencesBacterial PhysiologyAmino Acidslcsh:ScienceProtein MetabolismExtraction TechniquesMultidisciplinarybiologyOrganic CompoundsAntimicrobialsStreptomyces coelicolorTryptophanDrugsChemistryBiochemistryPhysical SciencesPhysiological DifferentiationResearch ArticleTryptophan BiosynthesiSmall Protein; Biosynthesis; Morpho-Physiological Differentiation: Streptomyces coelicolorBiosynthesisResearch and Analysis MethodsMicrobiologyStreptomycesActinorhodin03 medical and health sciencesBiosynthesisMicrobial ControlBacterial SporesPharmacology030102 biochemistry & molecular biologyOrganic Chemistrylcsh:RChemical CompoundsTryptophanTrpM; Small Protein; Tryptophan Biosynthesis; Morphological Differentiation; Physiological Differentiation; Streptomyces coelicolor A3(2); ProteomicsBiology and Life SciencesProteinsBacteriologybiology.organism_classificationAmino Acid MetabolismMetabolism030104 developmental biologychemistrylcsh:QMorphological DifferentiationTrpM
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