Open AccessCloning, expression, purification, crystallization and X‐ray analysis of inositol monophosphatase from Mus musculus and Homo sapiens
Author(s) -
Singh Nisha,
Halliday Amy C.,
Knight Matthew,
Lack Nathan A.,
Lowe Edward,
Churchill Grant C.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112035191
Subject(s) - inositol , phosphatidylinositol , cloning (programming) , biology , biochemistry , escherichia coli , chemistry , gene , signal transduction , receptor , computer science , programming language
Inositol monophosphatase (IMPase) catalyses the hydrolysis of inositol monophosphate to inositol and is crucial in the phosphatidylinositol (PI) signalling pathway. Lithium, which is the drug of choice for bipolar disorder, inhibits IMPase at therapeutically relevant plasma concentrations. Both mouse IMPase 1 ( Mm IMPase 1) and human IMPase 1 ( Hs IMPase 1) were cloned into pRSET5a, expressed in Escherichia coli , purified and crystallized using the sitting‐drop method. The structures were solved at resolutions of 2.4 and 1.7 Å, respectively. Comparison of Mm IMPase 1 and Hs IMPase 1 revealed a core r.m.s. deviation of 0.516 Å.