Crystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A(2) complexed with p-bromophenacyl bromide and alpha-tocopherol inhibitors at 1.9- and 1.45-A resolution

Biochim Biophys Acta. 2004 Jun 1;1699(1-2):281-4. doi: 10.1016/j.bbapap.2004.02.005.

Abstract

An acidic phospholipase A(2) (PLA(2)) isolated from Bothrops jararacussu snake venom was crystallized with two inhibitors: alpha-tocopherol (vitamin E) and p-bromophenacyl bromide (BPB). The crystals diffracted at 1.45- and 1.85-A resolution, respectively, for the complexes with alpha-tocopherol and p-bromophenacyl bromide. The crystals are not isomorphous with those of the native protein, suggesting the inhibitors binding was successful and changes in the quaternary structure may have occurred.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetophenones / metabolism*
  • Animals
  • Antioxidants / metabolism
  • Binding Sites
  • Bothrops*
  • Crotalid Venoms / chemistry
  • Crotalid Venoms / enzymology*
  • Crystallization
  • Enzyme Inhibitors / metabolism
  • Phospholipases A / chemistry*
  • Phospholipases A / metabolism*
  • Vitamin E / metabolism*
  • X-Ray Diffraction

Substances

  • Acetophenones
  • Antioxidants
  • Crotalid Venoms
  • Enzyme Inhibitors
  • Vitamin E
  • Phospholipases A
  • 4-bromophenacyl bromide