3ISO

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

3ISO の概要

• エントリーDOI: 10.2210/pdb3iso/pdb
• 分子名称: Putative glutathione transferase, GLUTATHIONE, ZINC ION, ... (5 entities in total)
• 機能のキーワード: gst, transferase
• 由来する生物種: Clonorchis sinensis (oriental liver fluke)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51645.15

構造登録者

Han, Y.H.,Seo, H.A.,Kim, G.H.,Chung, Y.J. (登録日: 2009-08-27, 公開日: 2010-09-08, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)