Crystallization and preliminary X-ray diffraction analysis of an L-amino-acid oxidase from Bothrops jararacussu venom.
Snake-venom L-amino-acid oxidases (SV-LAAOs) trigger a wide range of local and systematic effects, including inhibition of platelet aggregation, cytotoxicity, haemolysis, apoptosis and haemorrhage. These effects mainly arise from the uncontrolled release of the hydrogen peroxide that is produced by the redox reaction involving L-amino acids catalyzed by these flavoenzymes. Taking their clinical relevance into account, few SV-LAAOs have been structurally characterized and the structural determinants responsible for their broad direct and indirect pharmacological activities remain unclear. In this work, an LAAO from Bothrops jararacussu venom (BJu-LAAO) was purified and crystallized. The BJu-LAAO crystals belonged to space group P2(1), with unit-cell parameters a = 66.38, b = 72.19, c = 101.53 Å, β = 90.9°. The asymmetric unit contained two molecules and the structure was determined and partially refined at 3.0 Å resolution.
Centro Multiusuário de Inovação Biomolecular, Departamento de Física, Universidade Estadual Paulista (UNESP), São José do Rio Preto-SP, Brazil.
Anwar
A
Ullah
Monika
M
Coronado
Mário T
MT
Murakami
Christian
C
Betzel
Raghuvir K
RK
Arni
D000818:Animals; D017837:Bothrops; D003460:Crystallization; D018360:Crystallography, X-Ray; D050830:L-Amino Acid Oxidase / Q000737:chemistry*; D012910:Snake Venoms / Q000737:chemistry*
D012910:Snake Venoms; D050830:L-Amino Acid Oxidase