3ISO

Crystal structure of 26 kDa GST of Clonorchis sinensis in P3221 symmetry

Summary for 3ISO

• Entry DOI: 10.2210/pdb3iso/pdb
• Descriptor: Putative glutathione transferase, GLUTATHIONE, ZINC ION, ... (5 entities in total)
• Functional Keywords: gst, transferase
• Biological source: Clonorchis sinensis (oriental liver fluke)
• Total number of polymer chains: 2
• Total formula weight: 51645.15

Authors

Han, Y.H.,Seo, H.A.,Kim, G.H.,Chung, Y.J. (deposition date: 2009-08-27, release date: 2010-09-08, Last modification date: 2023-11-01)

Primary citation

Han, Y.H.,Seo, H.A.,Kim, G.H.,Lee, C.K.,Kang, Y.K.,Ryu, K.H.,Chung, Y.J.
A histidine substitution confers metal binding affinity to a Schistosoma japonicum Glutathione S-transferase.
Protein Expr.Purif., 73:74-77, 2010

PubMed Abstract: 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.

PubMed: 20347989
DOI: 10.1016/j.pep.2010.03.014

Experimental method

X-RAY DIFFRACTION (1.9 Å)