Nudix hydrolase

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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 Contents 1 Function 2 Relevance 3 Structural highlights 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[1]. 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[2]. 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[3]. Structural highlights The structure contains the NDX signature sequence and [4]. Monomer A is colored deepskyblue, monomer B is colored salmon, water molecules are shown as red spheres.

3D structures of Nudix hydrolase

Updated on 24-July-2019

2b0v, 3cng - NDX - Nitrosomonas europaea
1k2e, 1jrk, 1k26 - NDX (mutant) - Pyrobaculum aerophilum
1sjy, 1soi, 2w4e - DrNDX - Deinococcus radiodurans
1su2 - DrNDX + ATP
1sz3 - DrNDX + GNP
3fcm, 3f6a - NDX - Clostridium perfringens
3qsj - NDX - Alicyclobacillus acidocaldarius
3r03 - NDX - Rhodospirillum rubrum
2azw, 2fml - NDX - Enterococcus faecalis
2b06, 2pqv - NDX - Streptococcus pneumoniae
3exq - NDX - Lactobacillus brevis
3i9x - NDX - Listeria innocua
3id9, 3smd - NDX - Bacillus thuringiensis
4dyw - NDX - Burkholderia pseudomallei

References

1. ↑ McLennan AG. The Nudix hydrolase superfamily. Cell Mol Life Sci. 2006 Jan;63(2):123-43. doi: 10.1007/s00018-005-5386-7. PMID:16378245 doi:http://dx.doi.org/10.1007/s00018-005-5386-7
2. ↑ Sheikh S, O'Handley SF, Dunn CA, Bessman MJ. Identification and characterization of the Nudix hydrolase from the Archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose pyrophosphatase. J Biol Chem. 1998 Aug 14;273(33):20924-8. PMID:9694840
3. ↑ McLennan AG. The MutT motif family of nucleotide phosphohydrolases in man and human pathogens (review). Int J Mol Med. 1999 Jul;4(1):79-89. PMID:10373642
4. ↑ Ranatunga W, Hill EE, Mooster JL, Holbrook EL, Schulze-Gahmen U, Xu W, Bessman MJ, Brenner SE, Holbrook SR. Structural studies of the Nudix hydrolase DR1025 from Deinococcus radiodurans and its ligand complexes. J Mol Biol. 2004 May 21;339(1):103-16. PMID:15123424 doi:http://dx.doi.org/10.1016/j.jmb.2004.01.065