1ua5
From Proteopedia
Non-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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