Nudix hydrolase

spinqualitylabelsall models Structure of Nudix hydrolase MutT complex with ATP and Mg+2 ion (green) (PDB entry 1su2) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Nudix hydrolase (NDX) hydrolyses a wide range of organic pyrophosphatases including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps. In prokaryotes the number of Nudix genes varies from 0 to over 30. Mammals have around 24 Nudix genes. NDX proteins contain the GX5EX7REUXEEXGU signature sequence. An example of a well-studied Nudix enzyme is NudT16. Human NDX 16 is called U8-SNORNA-capping enzyme. Nudix hydrolase 7 has a role in peroxisomal acyl-CoA homeostasis. Nudix hydrolase 15 is a negative regulator of thiopurine activation and toxicity. Relevance NDX 7 eliminates potentially toxic nucleotide metabolites from the cell. The NDX of E. coli is named MutT and is able to neutralize the promutagenic compound 7,8-dihydro-oxoguanosine triphosphate thus preventing its incorporation into DNA. Structural highlights The structure contains the NDX signature sequence and the bound ligand is seen interacting with both monomers and with the Mg+2 ions. Monomer A is colored deepskyblue, monomer B is colored salmon, water molecules are shown as red spheres. 3D structures of Nudix hydrolase Nudix hydrolase 3D structures

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