Crystallization and preliminary X-ray diffraction studies of piratoxin II, a phospholipase A2 isolated from the venom of Bothrops pirajai

Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1437-9. doi: 10.1107/s0907444998007082.

Abstract

The phospholipases A2 (PLA2, E.C. 3.1.1.4, phosphatide sn2 acylhydrolases) are the major components of the venom of several snakes. They are responsible for several important pharmacological effects observed in ophidian incidents. PLA2 piratoxin II from Bothrops pirajai has been crystallized by the vapour-diffusion technique. X-ray diffraction data have been collected to 2.04 A resolution (90.2% complete, Rmerge = 0.070). The space group is P21 and the cell parameters are a = 46.19, b = 60.36, c = 58.74 A and beta = 96.05 degrees. The structure has been solved by molecular replacement using the crystallographic structure of PLA2 from Bothrops asper (PDB code 1CLP) as a search model.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bothrops / metabolism*
  • Chromatography, High Pressure Liquid
  • Crotalid Venoms / enzymology*
  • Crystallization
  • Crystallography, X-Ray
  • Dimerization
  • Group II Phospholipases A2
  • Molecular Weight
  • Phospholipases A / chemistry*
  • Phospholipases A / isolation & purification
  • Phospholipases A2
  • Protein Conformation
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / isolation & purification

Substances

  • Crotalid Venoms
  • Recombinant Fusion Proteins
  • Phospholipases A
  • Group II Phospholipases A2
  • Phospholipases A2
  • piratoxin II