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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):405-8. doi: 10.1107/S1744309108009111. Epub 2008 Apr 24.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Anthracenes
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Hypericum / chemistry*
  • Molecular Sequence Data
  • Perylene / analogs & derivatives*
  • Perylene / metabolism
  • Plant Proteins / chemistry*
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Sequence Homology, Amino Acid

Substances

  • Anthracenes
  • Plant Proteins
  • Perylene
  • hypericin