ADP-ribose pyrophosphatase

spinqualitylabelsall models ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, 1khz Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function ADP-ribose pyrophosphatase (ADPRP) or ADPRase catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them. ADPRP belongs to the family of NUDIX hydrolase. Structural highlights ADPRP contains two domains: the N-terminal domain responsible for dimer stabilization and the C-terminal which contains the active site. The C-terminal domain contains the Nudix (Nucleoside Diphosphate linked to X) sequence which is typical to pyrophosphatases and binds the metal ion. Residues from both monomers of ADPRP participate in the active site. Water molecules are shown as red spheres. Interactions of Mg+2 ion cluster. 1st Mg+2 ion coordination site. 2nd Mg+2 ion coordination site. 3rd Mg+2 ion coordination site. 3D structures of ADP-ribose pyrophosphatase ADP-ribose pyrophosphatase 3D structures

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