Yeast nucleus-localized thiol peroxidase(nTPx) is a functional peroxidase with two cysteine residues. For the structural analysis of reduced conformation of this protein, two cysteine residues are mutated by serine. The nTPx-mutant protein is crystall...
Yeast nucleus-localized thiol peroxidase(nTPx) is a functional peroxidase with two cysteine residues. For the structural analysis of reduced conformation of this protein, two cysteine residues are mutated by serine. The nTPx-mutant protein is crystallized by sparse matrix crystal screening using hanging drop method. Initial crystal has a rare hairy looking thin needle-like morphology. A series of optimization process was undertaken by a systematic approach. Traditional homology modeling technique is used for the prediction of nTPx-mutant protein. The predicted structure showed the typical thioredoxin fold with the topology which is similar with AhpC peroxiredoxin family. Compared with predicted nTPx structure, this enzyme system should have a typical 2-Cys redox mechanism.