This is the N-terminal domain found in trehalose-6-phosphate phosphatase (T6PP, EC 3.1.3.12) from parasitic nematodes such as Brugia malayi. In the model nematode Caenorhabditis elegans, T6PP is essential for survival due to the toxic effect(s) of th ...
This is the N-terminal domain found in trehalose-6-phosphate phosphatase (T6PP, EC 3.1.3.12) from parasitic nematodes such as Brugia malayi. In the model nematode Caenorhabditis elegans, T6PP is essential for survival due to the toxic effect(s) of the accumulation of trehalose 6-phosphate. T6PP has also been shown to be essential in Mycobacterium tuberculosis. The N-terminal domain composed of a three-helix bundle is similar in topology to the Microtubule Interacting and Transport (MIT) domains of the Vps4-like ATPases from Sulfolobus acidocaldarius. MIT domains are protein-interacting domains typically associated with multivesicular body formation, cytokinetic abscission, or viral budding. Mutational analysis indicate that deletion or mutation of the MIT-like domain is highly destabilizing to the enzyme [1].
This is the catalytic C-terminal domain of trehalose-6-phosphate phosphatase from parasitic nematodes such as Brugia malayi. This domain adopts a C2B-type HAD phosphatase fold [1]. In C. elegans, T6PP is essential for survival due to the toxic effect ...
This is the catalytic C-terminal domain of trehalose-6-phosphate phosphatase from parasitic nematodes such as Brugia malayi. This domain adopts a C2B-type HAD phosphatase fold [1]. In C. elegans, T6PP is essential for survival due to the toxic effect(s) of the accumulation of trehalose 6-phosphate.
