PMID:17725819

Citation	Brown, AK, Meng, G, Ghadbane, H, Scott, DJ, Dover, LG, Nigou, J, Besra, GS and Fütterer, K (2007) Dimerization of inositol monophosphatase Mycobacterium tuberculosis SuhB is not constitutive, but induced by binding of the activator Mg2+. BMC Struct. Biol. 7:55
Abstract	The cell wall of Mycobacterium tuberculosis contains a wide range of phosphatidyl inositol-based glycolipids that play critical structural roles and, in part, govern pathogen-host interactions. Synthesis of phosphatidyl inositol is dependent on free myo-inositol, generated through dephosphorylation of myo-inositol-1-phosphate by inositol monophosphatase (IMPase). Human IMPase, the putative target of lithium therapy, has been studied extensively, but the function of four IMPase-like genes in M. tuberculosis is unclear.
Links	PubMed PMC2080633 Online version:10.1186/1472-6807-7-55
Keywords	Apoproteins/chemistry; Apoproteins/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Crystallography, X-Ray; Dimerization; Magnesium/metabolism; Models, Molecular; Mycobacterium tuberculosis/classification; Mycobacterium tuberculosis/enzymology; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/metabolism; Protein Conformation; Protein Subunits/chemistry; Protein Subunits/metabolism
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