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Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum.

ABSTRACT: The opium poppy Papaver somniferum is the source of the narcotic analgesics morphine and codeine. Salutaridine reductase (SalR; EC 1.1.1.248) reduces the C-7 keto group of salutaridine to the C-7 (S)-hydroxyl group of salutaridinol in the biosynthetic pathway that leads to morphine in the opium poppy plant. P. somniferum SalR was overproduced in Escherichia coli and purified using cobalt-affinity and size-exclusion chromatography. Hexagonal crystals belonging to space group P6(4)22 or P6(2)22 were obtained using ammonium sulfate as precipitant and diffracted to a resolution of 1.9 A.

SUBMITTER: Higashi Y 

PROVIDER: S-EPMC2815683 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray diffraction analysis of salutaridine reductase from the opium poppy Papaver somniferum.

Higashi Yasuhiro Y   Smith Thomas J TJ   Jez Joseph M JM   Kutchan Toni M TM  

Acta crystallographica. Section F, Structural biology and crystallization communications 20100127 Pt 2

The opium poppy Papaver somniferum is the source of the narcotic analgesics morphine and codeine. Salutaridine reductase (SalR; EC 1.1.1.248) reduces the C-7 keto group of salutaridine to the C-7 (S)-hydroxyl group of salutaridinol in the biosynthetic pathway that leads to morphine in the opium poppy plant. P. somniferum SalR was overproduced in Escherichia coli and purified using cobalt-affinity and size-exclusion chromatography. Hexagonal crystals belonging to space group P6(4)22 or P6(2)22 we  ...[more]

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