Crystallization and high-resolution X-ray diffraction data collection of an Asp49 PLA2 from Bothrops jararacussu venom both in the presence and absence of Ca2+ ions

Biochim Biophys Acta. 2004 Dec 1;1703(1):79-81. doi: 10.1016/j.bbapap.2004.08.008.

Abstract

Snake venom PLA(2)s have been extensively studied due to their role in mediating and disrupting physiological processes such as coagulation, platelet aggregation and myotoxicity. The Ca(2+) ion bound to the putative calcium-binding loop is essential for hydrolytic activity. We report the crystallization in the presence and absence of Ca(2+) and X-ray diffraction data collection at 1.60 angstroms (with Ca(2+)) and 1.36 angstroms (without Ca(2+)) of an Asp49 PLA(2) from Bothrops jararacussu venom. The crystals belong to orthorhombic space group C222(1). Initial refinement and electron density analysis indicate significant conformational changes upon Ca(2+) binding.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Aspartic Acid / chemistry*
  • Bothrops*
  • Calcium / metabolism*
  • Crotalid Venoms / chemistry*
  • Crotalid Venoms / enzymology
  • Crystallography, X-Ray
  • Group II Phospholipases A2
  • Phospholipases A / chemistry*
  • Phospholipases A / isolation & purification
  • Phospholipases A / metabolism
  • Phospholipases A2
  • X-Ray Diffraction

Substances

  • Crotalid Venoms
  • Aspartic Acid
  • Phospholipases A
  • Group II Phospholipases A2
  • Phospholipases A2
  • Calcium