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Nudix hydrolase
From Proteopedia
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| - | <StructureSection load='1su2' size=' | + | <StructureSection load='1su2' size='400' side='right' caption='Structure of Nudix hydrolase MutT complex with ATP and Mg+2 ion (green) (PDB entry [[1su2]])' scene='48/488532/Cv/1'> |
__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. NDX proteins contain the GX5EX7REUXEEXGU signature sequence<ref>PMID:9694840</ref>. | + | '''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>. An example of a well-studied Nudix enzyme is [[NudT16]]. Human NDX 16 is called '''U8-SNORNA-capping enzyme'''. |
== Relevance == | == Relevance == | ||
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== 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>. | + | The structure contains the NDX signature sequence and <scene name='48/488532/Cv/5'>the bound ligand is seen interacting with both monomers and with the Mg+2 ions</scene><ref>PMID:15123424</ref>. Monomer A is colored deepskyblue, monomer B is colored salmon, water molecules are shown as red spheres. |
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| + | ==3D structures of Nudix hydrolase== | ||
| + | [[Nudix hydrolase 3D structures]] | ||
</StructureSection> | </StructureSection> | ||
| - | ==3D structures of Nudix hydrolase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
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| - | [[2b0v]], [[3cng]] - NDX - ''Nitrosomonas europaea''<br /> | ||
| - | [[1k2e]], [[1jrk]], [[1k26]] - NDX (mutant) - ''Pyrobaculum aerophilum''<br /> | ||
| - | [[1sjy]], [[1soi]], [[2w4e]] - DrNDX - ''Deinococcus radiodurans''<br /> | ||
| - | [[1su2]] - DrNDX + ATP <br /> | ||
| - | [[1sz3]] - DrNDX + GNP <br /> | ||
| - | [[3fcm]], [[3f6a]] - NDX - ''Clostridium perfringens'' <br /> | ||
| - | [[3qsj]] - NDX - ''Alicyclobacillus acidocaldarius''<br /> | ||
| - | [[3r03]] - NDX - ''Rhodospirillum rubrum'' <br /> | ||
| - | [[2azw]], [[2fml]] - NDX - ''Enterococcus faecalis''<br /> | ||
| - | [[2b06]], [[2pqv]] - NDX - ''Streptococcus pneumoniae'' <br /> | ||
| - | [[3exq]] - NDX - ''Lactobacillus brevis''<br /> | ||
| - | [[3i9x]] - NDX - ''Listeria innocua''<br /> | ||
| - | [[3id9]], [[3smd]] - NDX - ''Bacillus thuringiensis''<br /> | ||
| - | [[4dyw]] - NDX - ''Burkholderia pseudomallei''<br /> | ||
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== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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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
