ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the mitochondrial tryparedoxin peroxidase from Leishmania braziliensis.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Serine Proteinases in Leishmania (Viannia) braziliensis Promastigotes Have Distinct Subcellular Distributions and Expression.International journal of molecular sciences · 2019Article
- Calcium and magnesium ions modulate the oligomeric state and function of mitochondrial 2-Cys peroxiredoxins inThe Journal of biological chemistry · 2017Article
- How pH modulates the dimer-decamer interconversion of 2-Cys peroxiredoxins from the Prx1 subfamily.The Journal of biological chemistry · 2015Article
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Abstract
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.
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