6533b831fe1ef96bd129875b

RESEARCH PRODUCT

Vinorine synthase from Rauvolfia: the first example of crystallization and preliminary X-ray diffraction analysis of an enzyme of the BAHD superfamily

Hartmut MichelJoachim StöckigtJuergen KoepkeAnja BayerBin ZhangXueyan MaGünter FritzschVerena Linhard

subject

RauvolfiaIndolesStereochemistryBiophysicsCrystallography X-RayBiochemistryRauwolfiaAnalytical Chemistrychemistry.chemical_compoundAlkaloidsBiosynthesisRauvolfia serpentinamedicineMolecular Biologychemistry.chemical_classificationATP synthasebiologybiology.organism_classificationEnzymesAjmalineEnzymechemistryBiochemistryAcyltransferasesAcetyltransferasebiology.proteinCrystallizationmedicine.drug

description

Abstract Crystals of vinorine synthase (VS) from medicinal plant Rauvolfia serpentina expressed in Escherichia coli have been obtained by the hanging-drop technique at 305 K with ammonium sulfate and PEG 400 as precipitants. The enzyme is involved in the biosynthesis of the antiarrhythmic drug ajmaline and is a member of the BAHD superfamily of acyltransferases. So far, no three-dimensional structure of a member of this enzyme family is known. The crystals belong to the space group P 2 1 2 1 2 1 with cell dimensions of a =82.3 A, b =89.6 A and c =136.2 A. Under cryoconditions (120 K), a complete data set up to 2.8 A was collected at a synchrotron source.

yearjournalcountryeditionlanguage
2004-05-05Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
https://doi.org/10.1016/j.bbapap.2004.06.011