Crystallization and preliminary crystallographic studies of Hyp-1, a St John's wort protein implicated in the biosynthesis of hypericin.
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.
Fernandes
Humberto
H
Center for Biocrystallographic Research, Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
Konieczna
Malgorzata
M
Kolodziejczyk
Robert
R
Bujacz
Grzegorz
G
Sikorski
Michal
M
Jaskolski
Mariusz
M
D000595:Amino Acid Sequence; D000873:Anthracenes; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D020902:Hypericum / Q000737:chemistry*; D008969:Molecular Sequence Data; D010569:Perylene / Q000031:analogs & derivatives* / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
D000873:Anthracenes; D010940:Plant Proteins; D010569:Perylene; C004965:hypericin