1ua5
Non-fusion GST from S. japonicum in complex with glutathioneNon-fusion GST from S. japonicum in complex with glutathione
Structural highlights
FunctionGST26_SCHJA Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSchistosoma japonicum glutathione S-transferase (SjGST) is a common fusion tag in recombinant protein production, and its 3-dimensional structure has been studied in the context of drug design. We have determined the crystal structure of non-fused SjGST complexed with glutathione, and compare it to complexes between glutathione and SjGST fusion proteins. Crystal structure of non-fused glutathione S-transferase from Schistosoma japonicum in complex with glutathione.,Kursula I, Heape AM, Kursula P Protein Pept Lett. 2005 Oct;12(7):709-12. doi: 10.2174/0929866054696154. PMID:16522189[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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