Open AccessCrystallization and preliminary crystallographic studies of Hyp‐1, a St John's wort protein implicated in the biosynthesis of hypericin
Author(s) -
Fernandes Humberto,
Konieczna Malgorzata,
Kolodziejczyk Robert,
Bujacz Grzegorz,
Sikorski Michal,
Jaskolski Mariusz
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108009111
Subject(s) - hypericin , hypericum perforatum , orthorhombic crystal system , crystallization , biosynthesis , emodin , chemistry , escherichia coli , stereochemistry , hypericum , recombinant dna , crystallography , biochemistry , crystal structure , biology , organic chemistry , gene , botany , pharmacology
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 P 2 1 2 1 2 1 , with unit‐cell parameters a = 37.5, b = 76.7, c = 119.8 Å, contain two protein molecules in the asymmetric unit and diffract X‐rays to 1.73 Å resolution.