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

✍ Scribed by Xueyan Ma; Juergen Koepke; Anja Bayer; Verena Linhard; Günter Fritzsch; Bin Zhang; Hartmut Michel; Joachim Stöckigt

• Publisher: Elsevier Science
• Year: 2004
• Tongue: English
• Weight: 139 KB
• Volume: 1701
• Category: Article
• ISSN: 1570-9639
• DOI: 10.1016/j.bbapap.2004.06.011

✦ Synopsis

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 P2 1 2 1 2 1 with cell dimensions of a=82.3 2, b=89.6 2 and c=136.2 2. Under cryoconditions (120 K), a complete data set up to 2.8 2 was collected at a synchrotron source.