Open AccessPurification, crystallization and preliminary X‐ray analysis of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli
Author(s) -
Zheng Jimin,
Lee Daniel C.,
Jia Zongchao
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109014729
Subject(s) - isocitrate dehydrogenase , crystallization , escherichia coli , biochemistry , dehydrogenase , phosphatase , glyoxylate cycle , citric acid cycle , idh1 , phosphorylation , chemistry , microbiology and biotechnology , biology , enzyme , gene , organic chemistry , mutation
The Escherichia coli aceK gene encodes isocitrate dehydrogenase kinase/phosphatase (EC 2.7.11.5), a bifunctional protein that phosphorylates and dephosphorylates isocitrate dehydrogenase (IDH), resulting in its inactivation and activation, respectively. This reversible (de)phosphorylation directs isocitrate, an intermediate of the citric acid cycle, to either go through the full cycle or to enter the glyoxylate bypass. In the present study, the AceK protein from E. coli has been purified and crystallized. Three crystal forms were obtained from very similar crystallization conditions. The crystals belong to space groups P 4 1 2 1 2, P 3 2 21 and P 2 1 2 1 2 1 and diffracted X‐rays to resolutions of 2.9, 3.0 and 2.7 Å, respectively.