PMID:11807262
| Citation |
Hibi, T, Hisada, H, Nakatsu, T, Kato, H and Oda, J (2002) Escherichia coli B gamma-glutamylcysteine synthetase: modification, purification, crystallization and preliminary crystallographic analysis. Acta Crystallogr. D Biol. Crystallogr. 58:316-8 |
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| Abstract |
Escherichia coli B gamma-glutamylcysteine synthetase (gammaGCS) catalyzes the ATP-dependent coupling of L-Glu and L-Cys to form the glutathione precursor gamma-L-Glu-Cys and is a target for development of potential therapeutic agents. By introducing four point mutations of surface-exposed cysteine residues to serine, the gammaGCS was purified to homogeneity; single crystals have been obtained using the hanging-drop vapour-diffusion method with sodium formate. The gammaGCS crystal diffracted to 2.8 A and belongs to space group R3, with unit-cell parameters a = b = 326.7, c = 103.9 A. |
| Links | |
| Keywords |
Crystallization; Crystallography, X-Ray; Cysteine/genetics; Escherichia coli/enzymology; Escherichia coli/genetics; Glutamate-Cysteine Ligase/chemistry; Glutamate-Cysteine Ligase/genetics; Glutamate-Cysteine Ligase/isolation & purification; Maleimides/chemistry; Mutation; Protein Conformation; Serine/genetics; Sulfhydryl Compounds/chemistry |
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