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
收藏
页码：1640 / 1641
页数：2
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