Crystallization and preliminary X-ray crystallographic studies of a Lys49-phospholipase A2 homologue from Bothrops pirajai venom complexed with rosmarinic acid

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt 6):699-701. doi: 10.1107/S1744309110013709. Epub 2010 May 27.

Abstract

PrTX-I, a noncatalytic and myotoxic Lys49-phospholipase A(2) from Bothrops pirajai venom, was crystallized in the presence of the inhibitor rosmarinic acid (RA). This is the active compound in the methanolic extract of Cordia verbenacea, a plant that is largely used in Brazilian folk medicine. The crystals diffracted X-rays to 1.8 A resolution and the structure was solved by molecular-replacement techniques, showing electron density that corresponds to RA molecules at the entrance to the hydrophobic channel. The crystals belong to space group P2(1)2(1)2(1), indicating conformational changes in the structure after ligand binding: the crystals of all apo Lys49-phospholipase A(2) structures belong to space group P3(1)21, while the crystals of complexed structures belong to space groups P2(1) or P2(1)2(1)2(1).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bothrops / metabolism*
  • Cinnamates / chemistry*
  • Cinnamates / metabolism
  • Crotalid Venoms / chemistry*
  • Crotalid Venoms / metabolism
  • Crystallization
  • Crystallography, X-Ray
  • Depsides / chemistry*
  • Depsides / metabolism
  • Lysine / chemistry
  • Models, Molecular
  • Phospholipases A2 / chemistry*
  • Phospholipases A2 / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Rosmarinic Acid

Substances

  • Cinnamates
  • Crotalid Venoms
  • Depsides
  • Phospholipases A2
  • Lysine