5fso: Difference between revisions

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'''Unreleased structure'''


The entry 5fso is ON HOLD
==MTH1 substrate recognition: Complex with a methylaminopyrimidinedione.==
 
<StructureSection load='5fso' size='340' side='right' caption='[[5fso]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
Authors: Nissink, J.W.M., Bista, M., Breed, J., Carter, N., Embrey, K., Read, J., Phillips, C., Winter, J.J.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[5fso]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FSO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FSO FirstGlance]. <br>
Description: MTH1 substrate recognition: Complex with a methylaminopyrimidinedione.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=S76:6-(METHYLAMINO)-1H-PYRIMIDINE-2,4-DIONE'>S76</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fsi|5fsi]], [[5fsk|5fsk]], [[5fsl|5fsl]], [[5fsm|5fsm]], [[5fsn|5fsn]]</td></tr>
[[Category: Winter, J.J]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fso OCA], [http://pdbe.org/5fso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fso RCSB], [http://www.ebi.ac.uk/pdbsum/5fso PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fso ProSAT]</span></td></tr>
[[Category: Nissink, J.W.M]]
</table>
== Function ==
[[http://www.uniprot.org/uniprot/8ODP_HUMAN 8ODP_HUMAN]] Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP.<ref>PMID:10373420</ref> <ref>PMID:10608900</ref> <ref>PMID:11139615</ref> <ref>PMID:12857738</ref> <ref>PMID:22556419</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bista, M]]
[[Category: Bista, M]]
[[Category: Breed, J]]
[[Category: Carter, N]]
[[Category: Embrey, K]]
[[Category: Embrey, K]]
[[Category: Carter, N]]
[[Category: Nissink, J W.M]]
[[Category: Phillips, C]]
[[Category: Phillips, C]]
[[Category: Breed, J]]
[[Category: Read, J]]
[[Category: Read, J]]
[[Category: Winter, J J]]
[[Category: Hydrolase]]
[[Category: Nudt1]]

Revision as of 03:38, 19 January 2017

MTH1 substrate recognition: Complex with a methylaminopyrimidinedione.MTH1 substrate recognition: Complex with a methylaminopyrimidinedione.

Structural highlights

5fso is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[8ODP_HUMAN] Antimutagenic. Acts as a sanitizing enzyme for oxidized nucleotide pools, thus suppressing cell dysfunction and death induced by oxidative stress. Hydrolyzes 8-oxo-dGTP, 8-oxo-dATP and 2-OH-dATP, thus preventing misincorporation of oxidized purine nucleoside triphosphates into DNA and subsequently preventing A:T to C:G and G:C to T:A transversions. Able to hydrolyze also the corresponding ribonucleotides, 2-OH-ATP, 8-oxo-GTP and 8-oxo-ATP.[1] [2] [3] [4] [5]

References

  1. ↑ Fujikawa K, Kamiya H, Yakushiji H, Fujii Y, Nakabeppu Y, Kasai H. The oxidized forms of dATP are substrates for the human MutT homologue, the hMTH1 protein. J Biol Chem. 1999 Jun 25;274(26):18201-5. PMID:10373420
  2. ↑ Fujii Y, Shimokawa H, Sekiguchi M, Nakabeppu Y. Functional significance of the conserved residues for the 23-residue module among MTH1 and MutT family proteins. J Biol Chem. 1999 Dec 31;274(53):38251-9. PMID:10608900
  3. ↑ Fujikawa K, Kamiya H, Yakushiji H, Nakabeppu Y, Kasai H. Human MTH1 protein hydrolyzes the oxidized ribonucleotide, 2-hydroxy-ATP. Nucleic Acids Res. 2001 Jan 15;29(2):449-54. PMID:11139615
  4. ↑ Yoshimura D, Sakumi K, Ohno M, Sakai Y, Furuichi M, Iwai S, Nakabeppu Y. An oxidized purine nucleoside triphosphatase, MTH1, suppresses cell death caused by oxidative stress. J Biol Chem. 2003 Sep 26;278(39):37965-73. Epub 2003 Jul 10. PMID:12857738 doi:10.1074/jbc.M306201200
  5. ↑ Takagi Y, Setoyama D, Ito R, Kamiya H, Yamagata Y, Sekiguchi M. Human MTH3 (NUDT18) protein hydrolyzes oxidized forms of guanosine and deoxyguanosine diphosphates: comparison with MTH1 and MTH2. J Biol Chem. 2012 Jun 15;287(25):21541-9. doi: 10.1074/jbc.M112.363010. Epub 2012, May 3. PMID:22556419 doi:10.1074/jbc.M112.363010

5fso, resolution 1.67Å

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