Escherichia coli B γ-glutamylcysteine synthetase:: modification, purification, crystallization and preliminary crystallographic analysis

被引：11

作者：

Hibi, T ^{[1
]}

Hisada, H

Nakatsu, T

Kato, H

Oda, J

机构：

[1] Fukui Prefectural Univ, Dept Biosci, Fukui 9101195, Japan

[2] Kyoto Univ, Inst Chem Res, Uji, Kyoto 6110011, Japan

[3] RIKEN, SPring 8, Harima Inst, Membrane Dynam Res Grp, Sayo, Hyogo 6795148, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2002年 / 58卷

关键词：

D O I：

10.1107/S0907444901019886

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 GCS crystal diffracted to 2.8 Angstrom and belongs to space group R3, with unit-cell parameters a = b = 326.7, c = 103.9 Angstrom.

引用

页码：316 / 318

页数：3

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