Structural highlights
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 PubMed
Glutathione S-transferases (GSTs) are multifunctional enzymes that are used as fusion tags on recombinant proteins in mammalian and Escherichia coli expression systems. We recently found that the Schistosoma japonicum GST (SjGST) displays weak Ni(2+) ion binding affinity. Glu26 and His79 were assumed to be its Ni(2+) binding sites based on the structure of the 26-kDa Clonorchis sinensis GST. To enhance SjGST Ni(2+) binding affinity, Glu26 was mutated to His. SjGST-E26H was expressed and purified at a high concentration of imidazole to a higher purity than wild type SjGST. In addition, human biotin protein ligase fused to SjGST-E26H was purified with a immobilized Ni affinity column.
A histidine substitution confers metal binding affinity to a Schistosoma japonicum Glutathione S-transferase.,Han YH, Seo HA, Kim GH, Lee CK, Kang YK, Ryu KH, Chung YJ Protein Expr Purif. 2010 Sep;73(1):74-7. Epub 2010 Mar 27. PMID:20347989[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Han YH, Seo HA, Kim GH, Lee CK, Kang YK, Ryu KH, Chung YJ. A histidine substitution confers metal binding affinity to a Schistosoma japonicum Glutathione S-transferase. Protein Expr Purif. 2010 Sep;73(1):74-7. Epub 2010 Mar 27. PMID:20347989 doi:10.1016/j.pep.2010.03.014
