Heterologous expression, purification, crystallization and preliminary X-ray analysis of raucaffricine glucosidase, a plant enzyme specifically involved in Rauvolfia alkaloid biosynthesis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt 3):257-60. doi: 10.1107/S174430910600457X. Epub 2006 Feb 24.

Abstract

Raucaffricine glucosidase (RG) is an enzyme that is specifically involved in the biosynthesis of indole alkaloids from the plant Rauvolfia serpentina. After heterologous expression in Escherichia coli cells, crystals of RG were obtained by the hanging-drop vapour-diffusion technique at 293 K with 0.3 M ammonium sulfate, 0.1 M sodium acetate pH 4.6 buffer and 11% PEG 4000 as precipitant. Crystals belong to space group I222 and diffract to 2.30 A, with unit-cell parameters a = 102.8, b = 127.3, c = 215.8 A.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cloning, Molecular
  • Crystallization / methods
  • Crystallography, X-Ray
  • Escherichia coli / metabolism
  • Glucosidases / biosynthesis
  • Glucosidases / chemistry*
  • Glucosidases / isolation & purification
  • Rauwolfia / enzymology

Substances

  • Glucosidases
  • raucaffricine beta-glucosidase