1. Expression, characterization and crystal structure of thioredoxin fromSchistosoma japonicum
- Author
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Xiaolin Fan, Qunfeng Wu, Xun Li, Dashuang Shi, Yun Peng, Daoyi Guo, Fuyan Huang, Hui Zhou, Xiao-Nong Zhou, Yongdong Li, Pan Li, and Xiang Liu
- Subjects
Models, Molecular ,Molecular Sequence Data ,Gene Expression ,Reductase ,Thioredoxin fold ,medicine.disease_cause ,Schistosoma japonicum ,Dithiothreitol ,chemistry.chemical_compound ,Thioredoxins ,Multienzyme Complexes ,Oxidoreductase ,parasitic diseases ,Escherichia coli ,medicine ,Animals ,Humans ,NADH, NADPH Oxidoreductases ,Amino Acid Sequence ,chemistry.chemical_classification ,biology ,Helminth Proteins ,biology.organism_classification ,Recombinant Proteins ,Infectious Diseases ,chemistry ,Biochemistry ,Female ,Animal Science and Zoology ,Parasitology ,Thioredoxin ,Oxidation-Reduction ,Sequence Alignment ,Function (biology) - Abstract
SUMMARYSchistosoma japonicum, a human blood fluke, causes a parasitic disease affecting millions of people in Asia. Thioredoxin–glutathione system ofS. japonicumplays a critical role in maintaining the redox balance in parasite, which is a potential target for development of novel antischistosomal agents. Here we cloned the gene ofS. japonicumthioredoxin (SjTrx), expressed and purified the recombinant SjTrx inEscherichia coli. Functional assay shows that SjTrx catalyses the dithiothreitol (DTT) reduction of insulin disulphide bonds. The coupling assay of SjTrx with its endogenous reductase, thioredoxin glutathione reductase fromS. japonicum(SjTGR), supports its biological function to maintain the redox homeostasis in the cell. Furthermore, the crystal structure of SjTrx in the oxidized state was determined at 2·0 Å resolution, revealing a typical architecture of thioredoxin fold. The structural information of SjTrx provides us important clues for understanding the maintenance function of redox homeostasis inS. japonicumand pathogenesis of this chronic disease.
- Published
- 2015
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