Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine.
Strictosidine synthase (STR1) is a central enzyme that participates in the biosynthesis of almost all plant monoterpenoid indole alkaloids. After heterologous expression in Escherichia coli, crystals of STR1 and its substrate complex with tryptamine were obtained by the hanging-drop technique at 302-304 K with potassium sodium tartrate tetrahydrate as precipitant. All crystals belong to space group R3. The native STR1 crystals diffract to 2.95 A and have unit-cell parameters a = b = 150.3, c = 122.4 A. The tryptamine complex crystals diffract to 2.38 A, with unit-cell parameters a = b = 147.3, c = 122.3 A.
Koepke
Juergen
J
Department of Molecular Membrane Biology, Max-Planck-Institute of Biophysics, Marie-Curie-Strasse 15, D-60439 Frankfurt/Main, Germany.
Ma
Xueyan
X
Fritzsch
Günter
G
Michel
Hartmut
H
Stöckigt
Joachim
J
D019759:Carbon-Nitrogen Lyases / Q000737:chemistry*; D003460:Crystallization; D010940:Plant Proteins / Q000737:chemistry*; D011926:Rauwolfia / Q000201:enzymology*; D014363:Tryptamines / Q000737:chemistry*
D010940:Plant Proteins; D014363:Tryptamines; C030820:tryptamine; D019759:Carbon-Nitrogen Lyases; C022684:strictosidine synthetase