Open AccessCrystallization and preliminary X‐ray diffraction studies of BmooPLA 2 ‐I, a platelet‐aggregation inhibitor and hypotensive phospholipase A 2 from Bothrops moojeni venom
Author(s) -
Salvador Guilherme H. M.,
MarchiSalvador Daniela P.,
Silveira Lucas B.,
Soares Andreimar M.,
Fontes Marcos R. M.
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911102392x
Subject(s) - bothrops , phospholipase , venom , snake venom , enzyme , hydrolysis , chemistry , phospholipase a2 , dynamic light scattering , monomer , phosphatidylcholine , biochemistry , phospholipid , membrane , organic chemistry , materials science , nanotechnology , nanoparticle , polymer
Phospholipases A 2 (PLA 2 s) are enzymes that cause the liberation of fatty acids and lysophospholipids by the hydrolysis of membrane phospholipids. In addition to their catalytic action, a wide variety of pharmacological activities have been described for snake‐venom PLA 2 s. BmooPLA 2 ‐I is an acidic, nontoxic and catalytic PLA 2 isolated from Bothrops moojeni snake venom which exhibits an inhibitory effect on platelet aggregation, an immediate decrease in blood pressure, inducing oedema at a low concentration, and an effective bactericidal effect. BmooPLA 2 ‐I has been crystallized and X‐ray diffraction data have been collected to 1.6 Å resolution using a synchrotron‐radiation source. The crystals belonged to space group C 222 1 , with unit‐cell parameters a = 39.7, b = 53.2, c = 89.2 Å. The molecular‐replacement solution of BmooPLA 2 ‐I indicated a monomeric conformation, which is in agreement with nondenaturing electrophoresis and dynamic light‐scattering experiments. A comparative study of this enzyme with the acidic PLA 2 from B. jararacussu (BthA‐I) and other toxic and nontoxic PLA 2 s may provide important insights into the functional aspects of this class of proteins.