4I8B

Crystal Structure of Thioredoxin from Schistosoma Japonicum

Summary for 4I8B

• Entry DOI: 10.2210/pdb4i8b/pdb
• Related: 2xbi
• Descriptor: Thioredoxin (2 entities in total)
• Functional Keywords: thioredoxin fold, protein-disulfide reductase, oxidoreductase
• Biological source: Schistosoma japonicum (Blood fluke)
• Total number of polymer chains: 2
• Total formula weight: 23474.76

Authors

Wu, Q.,Peng, Y.,Zhao, J.,Li, X.,Fan, X.,Zhou, X.,Chen, J.,Luo, Z.,Shi, D. (deposition date: 2012-12-03, release date: 2013-12-04, Last modification date: 2024-11-20)

Primary citation

Li, Y.,Li, P.,Peng, Y.,Wu, Q.,Huang, F.,Liu, X.,Li, X.,Zhou, H.,Guo, D.,Shi, D.,Zhou, X.N.,Fan, X.
Expression, characterization and crystal structure of thioredoxin from Schistosoma japonicum.
Parasitology, 142:1044-1052, 2015

PubMed Abstract: Schistosoma japonicum, a human blood fluke, causes a parasitic disease affecting millions of people in Asia. Thioredoxin-glutathione system of S. japonicum plays 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 of S. japonicum thioredoxin (SjTrx), expressed and purified the recombinant SjTrx in Escherichia 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 from S. 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 in S. japonicum and pathogenesis of this chronic disease.

PubMed: 25810021
DOI: 10.1017/S0031182015000244

Experimental method

X-RAY DIFFRACTION (2 Å)