Abstract
Snake venom PLA 2s have been extensively studied due to their role in mediating and disrupting physiological processes such as coagulation, platelet aggregation and myotoxicity. The Ca 2+ ion bound to the putative calcium-binding loop is essential for hydrolytic activity. We report the crystallization in the presence and absence of Ca 2+ and X-ray diffraction data collection at 1.60 Å (with Ca 2+) and 1.36 Å (without Ca 2+) of an Asp49 PLA 2 from Bothrops jararacussu venom. The crystals belong to orthorhombic space group C222 1. Initial refinement and electron density analysis indicate significant conformational changes upon Ca 2+ binding.
Published Version
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