Literature DB >> 18453712

Crystallization and preliminary crystallographic studies of Hyp-1, a St John's wort protein implicated in the biosynthesis of hypericin.

Humberto Fernandes1, Malgorzata Konieczna, Robert Kolodziejczyk, Grzegorz Bujacz, Michal Sikorski, Mariusz Jaskolski.   

Abstract

According to a debated hypothesis, the biosynthesis from emodin of the medicinally important natural compound hypericin is catalyzed in St John's wort (Hypericum perforatum) by the phenolic oxidative-coupling protein Hyp-1. Recombinant St John's wort Hyp-1 has been overexpressed in Escherichia coli and obtained in single-crystal form. The crystals belong to the orthorhombic system, space group P2(1)2(1)2(1), with unit-cell parameters a = 37.5, b = 76.7, c = 119.8 A, contain two protein molecules in the asymmetric unit and diffract X-rays to 1.73 A resolution.

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Year:  2008        PMID： 18453712      PMCID： PMC2376394          DOI： 10.1107/S1744309108009111

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


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  2 in total

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