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Crystallization and preliminary X‐ray diffraction studies of an L‐amino‐acid oxidase from Lachesis muta venom
Author(s) -
Ullah Anwar,
Masood Rehana,
Spencer Patrick Jack,
Murakami Mário Tyago,
Arni Raghuvir Krishnaswamy
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14017877
Subject(s) - venom , haemolysis , biochemistry , snake venom , stereochemistry , amino acid , oxidase test , biology , amino acid residue , chemistry , enzyme , microbiology and biotechnology , peptide sequence , immunology , gene
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 P 2 1 , 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.