Crystallization and preliminary X-ray crystallographic studies of phosphoenolpyruvate carboxykinase from Corynebacterium glutamicum

被引：3

作者：

Aich, S ^{[1
]}

Imabayashi, F ^{[1
]}

Delbaere, LTJ ^{[1
]}

机构：

[1] Univ Saskatchewan, Dept Biochem, Saskatoon, SK S7N 5E5, Canada

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷

关键词：

D O I：

10.1107/S0907444903014112

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Phosphoenolpyruvate carboxykinase (PCK) is a key enzyme involved in the regulation of gluconeogenesis. PCKs from higher animals require guanosine nucleotide for activity. PCK from Corynebacterium glutamicum is also GTP specific. X-ray diffraction data from a C. glutamicum PCK crystal were collected to 2.8 Angstrom resolution. The crystals were monoclinic, belonging to space group P2(1), with unit-cell parameters a = 71.7, b = 117.4, c = 161.3 Angstrom, beta = 92.9degrees. The presence of two molecules in the crystallographic asymmetric unit gives a V-M of 2.5 Angstrom(3) Da(-1) and a solvent content of 50.3%.

引用

页码：1640 / 1641

页数：2

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