Nudix hydrolase
From Proteopedia
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| - | <StructureSection load='1su2' size='350' side='right' caption='Structure of | + | <StructureSection load='1su2' size='350' side='right' caption='Structure of Nudix hydrolase MutT complex with ATP and Mg+2 ion (green) (PDB entry [[1su2]])' scene=''> |
__TOC__ | __TOC__ | ||
== Function == | == 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<ref>PMID:16378245</ref>. In prokaryotes the number of Nudix genes varies from 0 to over 30. Mammals have around 24 Nudix genes. | + | '''Nudix hydrolase''' (NDX) hydrolyses a wide range of organic pyrophosphatases including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps<ref>PMID:16378245</ref>. 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<ref>PMID:9694840</ref>. |
== Relevance == | == 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<ref>PMID:10373642</ref>. | + | 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<ref>PMID:10373642</ref>. |
== Structural highlights == | == 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<ref>PMID:15123424</ref>. | |
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</StructureSection> | </StructureSection> | ||
Revision as of 11:16, 4 November 2018
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3D structures of Nudix hydrolase
Updated on 04-November-2018
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
- ↑ 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
- ↑ 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
- ↑ 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
- ↑ 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
