A cartoon of the tertiary structure of TIGAR. TIGAR is approximately 30kDa and has a tertiary structure that is similar to the histidine phosphatase fold. The core of TIGAR is made up of an α-β-α sandwich, which consists of a six-stranded β sheet surrounded by 4 α helices. Additional α helices and a long loop are built around the core to give the full enzyme. TIGAR has an active site that is structurally similar to that of PhoE (a bacterial phosphatase enzyme) and functionally similar to that of fructose-2,6-bisphosphatase. The bis-phosphatase-like active site of TIGAR is positively charged, and catalyses the removal of phosphate groups from other molecules. In contrast to Fructose-2,6-Bisphosphatase, TIGAR's active site is open and accessible like that of PhoE. The site contains 3 crucial amino acids (2 histidines and 1 glutamic acid) that are involved in the phosphatase reaction. These 3 residues are known collectively as a catalytic triad, and are found in all enzymes belonging to the phosphoglyceromutase branch of the histidine phosphatase superfamily. One of the histidine residues is electrostatically bound to a negatively charged phosphate. A second phosphate is bound elsewhere in the active site.
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