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.
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.
Murakami
Mário T
MT
Departamento de Física, IBILCE, Universidade Estadual Paulista, R. Cristóvão Colombo 2265, Nazareth, CEP 15054-000, São José do Rio Preto, SP, Brazil.
Michelan-Duarte
Simone
S
Cintra
Adélia C O
AC
Arni
Raghuvir K
RK
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
D003435:Crotalid Venoms; D001224:Aspartic Acid; D010741:Phospholipases A; D054501:Group II Phospholipases A2; D054467:Phospholipases A2; D002118:Calcium