Search results for "Selenomethionine"

showing 3 items of 3 documents

Selenomethionine labeling of large biological macromolecular complexes: probing the structure of marine bacterial virus PM2.

2008

There is a need for improved tools for labeling protein species within large macromolecular assemblies. Here we describe a method for the efficient selenomethionine labeling of the membrane-containing bacterial virus PM2 for structural studies. By examining potential host cells a strain was found which was auxotrophic for methionine, and by performing a multiparameter search of conditions it was possible to derive a robust protocol which simultaneously minimized the toxic effects of the selenomethionine, so that a reasonable virus yield was maintained, whilst still achieving essentially complete labeling. This has allowed us to fingerprint the protein constituents of the virus in a relative…

0303 health sciencesbiologyStrain (chemistry)030306 microbiologyAuxotrophyCorticoviridaechemistry.chemical_elementCrystallography X-Raybiology.organism_classificationVirusBacteriophage03 medical and health scienceschemistryBiochemistryStructural BiologyYield (chemistry)MethodsBacterial virusSelenomethionineSelenium030304 developmental biologyMacromoleculeJournal of structural biology
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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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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