Crystallization and preliminary X-ray diffraction studies of an L-amino-acid oxidase from Lachesis muta venom.

Abstract

Snake-venom proteins form multi-component defence systems by the recruitment and rapid evolution of nonvenomous proteins and hence serve as model systems to understand the structural modifications that result in toxicity. L-Amino-acid oxidases (LAAOs) are encountered in a number of snake venoms and have been implicated in the inhibition of platelet aggregation, cytotoxicity, haemolysis, apoptosis and haemorrhage. An L-amino-acid oxidase from Lachesis muta venom has been purified and crystallized. The crystals belonged to space group P2₁, with unit-cell parameters a=66.05, b=79.41, c=100.52 Å, β=96.55°. The asymmetric unit contained two molecules and the structure has been determined and partially refined at 3.0 Å resolution.