Crystallization and preliminary X-ray diffraction studies of an L-amino-acid oxidase from Lachesis muta venom.
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.
Department of Physics, UNESP/IBILCE, Rua Cristovão Colombo 2265, São José Do Rio Preto, São Paulo 15054-000, Brazil.
Anwar
A
Ullah
Department of Physics, UNESP/IBILCE, Rua Cristovão Colombo 2265, São José Do Rio Preto, São Paulo 15054-000, Brazil.
Rehana
R
Masood
Comissão Nacional de Energia Nuclear, Instituto de Pesquisas Energéticas e Nucleares, IPEN, São Paulo 05508-900, Brazil.
Patrick Jack
PJ
Spencer
Laboratório Nacional de Biociências (LNBio), Centro Nacional de Pesquisa em Energia e Materiais, Campinas 13083-970, Brazil.
Mário Tyago
MT
Murakami
Department of Physics, UNESP/IBILCE, Rua Cristovão Colombo 2265, São José Do Rio Preto, São Paulo 15054-000, Brazil.
Raghuvir Krishnaswamy
RK
Arni
D000818:Animals; D003460:Crystallization; D050830:L-Amino Acid Oxidase / Q000737:chemistry* / Q000302:isolation & purification; D014757:Viper Venoms / Q000737:chemistry* / Q000201:enzymology*; D017819:Viperidae; D014961:X-Ray Diffraction
D014757:Viper Venoms; D050830:L-Amino Acid Oxidase
Lachesis muta; l-amino-acid oxidase