6533b830fe1ef96bd12966ad
RESEARCH PRODUCT
Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina.
Joachim StöckigtHartmut MichelGünter FritzschJuergen KoepkeAnja BayerXueyan Masubject
StereochemistryCrystallography X-RayRauwolfialaw.inventionIndole AlkaloidsLigaseschemistry.chemical_compoundBiosynthesisStructural BiologylawRauvolfia serpentinamedicineCrystallizationSelenomethioninePlant ProteinsPEG 400chemistry.chemical_classificationATP synthasebiologyGeneral Medicinebiology.organism_classificationAjmalineEnzymechemistryAcyltransferasesbiology.proteinCrystallizationmedicine.drugdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2005-05-26 | Acta crystallographica. Section D, Biological crystallography |