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

• Published in: Biochimica et biophysica acta Vol. 1699; no. 1-2; p. 281
• Main Authors: Takeda, Agnes A S, dos Santos, Juliana I, Marcussi, Silvana, Silveira, Lucas B, Soares, Andreimar M, Fontes, Marcos R M
• Format: Journal Article
• Language: English
• Published: Netherlands 01-06-2004
• Subjects: 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
• ISSN: 0006-3002
• DOI: 10.1016/j.bbapap.2004.02.005

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.