Article
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the mitochondrial tryparedoxin peroxidase from Leishmania braziliensis
Registro en:
MORAIS, Mariana Abrahão Bueno de et al. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the mitochondrial tryparedoxin peroxidase from Leishmania braziliensis. Acta Crystallogr. Sect F. Struct. Biol. Cryst. Commun, n. 69, p. 408-411.
1744-3091
10.1107/S1744309113003989
Autor
Morais, Mariana Abrahão Bueno de
Souza, Tatiana de Arruda Campos Brasil de
Murakami, Mario Tyago
Resumen
This research was supported by grants from Fundação de Amparo a Pesquisa do Estado de São Paulo (FAPESP), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) and Coordenação
de Aperfeiçoamento de Pessoal de Nível Superior (CAPES). Tryparedoxin peroxidase (TXNPx) is an essential constituent of the main enzymatic scavenger system for reactive oxygen species (ROS) in trypanosomatids. Genetic studies have demonstrated the importance of this system for the development and virulence of these parasites, representing a potential target for the discovery of new trypanocidal drugs. In this work, the mitochondrial TXNPx from Leishmania braziliensis was cloned, overexpressed, purified and crystallized. The crystals diffracted to 3.3 Å resolution and belonged to space group P4(2)2(1)2, with unit-cell parameters a = b = 131.8, c = 44.4 Å. These studies will contribute to a better understanding of the molecular mechanisms involved in ROS detoxification by trypanosomatids.