Crystallization and Preliminary X-ray Diffraction Studies of BmooPLA2-I, a Platelet-aggregation Inhibitor and Hypotensive Phospholipase A2 from Bothrops Moojeni Venom

Overview

Journal Acta Crystallogr Sect F Struct Biol Cryst Commun

Date 2011 Aug 9

PMID 21821890

Authors

Guilherme H M Salvador

Daniela P Marchi-Salvador

Lucas B Silveira

Andreimar M Soares

Marcos R M Fontes

Affiliations

Soon will be listed here.

Abstract

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 C222(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.

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