Crystallization and preliminary X-ray analysis of native and selenomethionyl vinorine synthase from Rauvolfia serpentina.
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 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 82.3, b = 89.6, c = 136.2 A. The selenomethionyl VS crystal was nearly isomorphous with the VS crystal.
Ma
Xueyan
X
Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University Mainz, Staudinger Weg 5, D-55099 Mainz, Germany.
Koepke
Juergen
J
Bayer
Anja
A
Fritzsch
Günter
G
Michel
Hartmut
H
Stöckigt
Joachim
J
D003460:Crystallization; D018360:Crystallography, X-Ray; D026121:Indole Alkaloids / Q000737:chemistry*; D008025:Ligases / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011926:Rauwolfia / Q000201:enzymology*; D012645:Selenomethionine / Q000737:chemistry*
D026121:Indole Alkaloids; D010940:Plant Proteins; C493776:vinorine; D012645:Selenomethionine; D008025:Ligases