title: Crystallization and high-resolution X-ray diffraction data collection of an Asp49 PLA2 from Bothrops jararacussu venom both in the presence and absence of Ca2+ ions.
abstract: Snake venom PLA(2)s 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 angstroms (with Ca(2+)) and 1.36 angstroms (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.
authors.affiliation: Departamento de Física, IBILCE, Universidade Estadual Paulista, R. Cristóvão Colombo 2265, Nazareth, CEP 15054-000, São José do Rio Preto, SP, Brazil.
authors.forename: Mário T
authors.initials: MT
authors.lastname: Murakami
authors.forename: Simone
authors.initials: S
authors.lastname: Michelan-Duarte
authors.forename: Adélia C O
authors.initials: AC
authors.lastname: Cintra
authors.forename: Raghuvir K
authors.initials: RK
authors.lastname: Arni
mesh_terms: D000818:Animals; D001224:Aspartic Acid / Q000737:chemistry*; D017837:Bothrops; D002118:Calcium / Q000378:metabolism*; D003435:Crotalid Venoms / Q000737:chemistry* / Q000201:enzymology; D018360:Crystallography, X-Ray; D054501:Group II Phospholipases A2; D010741:Phospholipases A / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D054467:Phospholipases A2; D014961:X-Ray Diffraction
chemical_list: D003435:Crotalid Venoms; D001224:Aspartic Acid; D010741:Phospholipases A; D054501:Group II Phospholipases A2; D054467:Phospholipases A2; D002118:Calcium