Crystallization and preliminary X-ray analysis of the β-isoform of glutamate decarboxylase from Escherichia coli

被引:5
作者
Malashkevich, VN
De Biase, D
Markovic-Housley, Z
Schlunegger, MP
Bossa, F
Jansonius, JN
机构
[1] Univ Basel, Biozentrum, CH-4056 Basel, Switzerland
[2] Univ Roma La Sapienza, CNR, Dipartimento Sci Biochim A Rossi Fanelli, I-00185 Rome, Italy
[3] Univ Roma La Sapienza, CNR, Ctr Biol Mol, I-00185 Rome, Italy
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 1998年 / 54卷
关键词
D O I
10.1107/S0907444998003497
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Glutamate decarboxylase (GAD) is a vitamin B-6 enzyme which catalyzes the alpha-decarboxylation of L-glutamate to gamma-aminobutyric acid (GABA). Escherichia coli cells coexpress two highly homologous enzyme isoforms, GAD alpha and GAD beta. Well diffracting crystals of GAD beta were obtained by taking advantage of the possibility of expressing each isoform separately. They belong to space group P3(1) or P3(2) with the unit-cell dimensions a = b = 115.6 and c = 206.6 Angstrom and contain one GAD hexamer in the asymmetric unit. High-resolution synchrotron data were collected at 100 K for the native protein and a potential heavy-atom derivative.
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收藏
页码:1020 / 1022
页数:3
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