Crystallization and preliminary X-ray analysis of strictosidine synthase and its complex with the substrate tryptamine

被引：16

作者：

Koepke, J

Ma, XY

Fritzsch, U

Michel, H

Stöckigt, J

机构：

[1] Johannes Gutenberg Univ Mainz, Inst Pharm, Dept Pharmaceut Biol, D-55099 Mainz, Germany

[2] Max Planck Inst Biophys, Dept Mol Membrane Biol, D-60439 Mainz, Germany

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2005年 / 61卷

关键词：

D O I：

10.1107/S0907444904029348

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom and have unit-cell parameters a = b = 150.3. c= 122.4 angstrom. The tryptamine complex crystals diffract to 2.38 angstrom, with unit-cell parameters a = b = 147.3, c = 122.3 angstrom.

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页码：690 / 693

页数：4

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