Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina
| Autor: | Joachim Stöckigt, Hartmut Michel, Günter Fritzsch, Juergen Koepke, Anja Bayer, Xueyan Ma |
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| Rok vydání: | 2004 |
| Předmět: |
Stereochemistry
Crystallography X-Ray Rauwolfia law.invention Indole Alkaloids Ligases chemistry.chemical_compound Biosynthesis Structural Biology law Rauvolfia serpentina medicine Crystallization Selenomethionine Plant Proteins PEG 400 chemistry.chemical_classification ATP synthase biology General Medicine biology.organism_classification Ajmaline Enzyme chemistry Acyltransferases biology.protein medicine.drug |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 61(Pt 6) |
| ISSN: | 0907-4449 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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