Deoxyuridine 5'-triphosphate nucleotidohydrolase: Difference between revisions

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{{STRUCTURE_1seh|  PDB=1seh  | SIZE=400| SCENE= |right|CAPTION=''E. coli''  dUTPase complex with dUTP [[1seh]] }}
<StructureSection load='1w2y' size='350' side='right' caption='dUTPase complex with dUTP analog and Mg+2 ions (green) (PDB entry [[1w2y]])' scene='48/488500/Cv/1'>


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'''Deoxyuridine 5’-triphosphate nucleotidohydrolase''' (DUTP) catalyzes the conversion of dUTP to dUMP and pyrophosphate (PPi).  DUTP plays a key role in keeping significant amounts of dUTP from the DNA synthesis pathway.  DUTP inhibitors are being tested as possible anti-bacterial agents targeting diseases like malaria, leishmaniasis, tuberculosis and trypanosomiasis.  Prokaryotic DUTP contains metal ion.


==3D structures of dUTPase==
'''Deoxyuridine 5’-triphosphate nucleotidohydrolase''' or '''Deoxyuridine triphosphatase''' or '''dUTP pyrophosphatase''' (DUTP) catalyzes the conversion of dUTP to dUMP and pyrophosphate (PPi).  DUTP plays a key role in keeping significant amounts of dUTP from the DNA synthesis pathway.
Prokaryotic DUTP contains metal ion. <ref>PMID:18837522</ref>
 
== Relevance ==
 
DUTP inhibitors are being tested as possible anti-bacterial agents targeting diseases like malaria, leishmaniasis, tuberculosis and trypanosomiasis. 


[[1dup]], [[1eu5]], [[1euw]] – EcDUTP – ''Escherichia coli''<br />
== Structural highlights ==
[[1dun]] – EvDUTP – Equine infectious anemia virus<br />
[[1mq7]] – MtDUTP – ''Mycobacterium tuberculosis''<br />
[[1ogl]] – TcDUTP – ''Trypanosoma cruzi''<br />
[[2d4l]] - MPmvDUTP residues 83-234 – Mason_Pfizer monkey virus<br />
[[2d4m]] - MPmvDUTP residues 83-234 (mutant) <br />
[[2okb]], [[2okd]] - VvDUTP – Vaccinia virus<br />
[[3hhq]] - yDUTP – yeast<br />
[[3lqw]] - DUTP – ''Entamoeba histolytica''<br />
[[3mbq]], [[3mdx]] - DUTP – ''Brucella melitensis''<br />
[[2xx6]] - BsDUTP – ''Bacillus subtilis''<br />
[[3tqz]] - DUTP – ''Coxiella burnetii''


'''DUTP binary complexes'''
The <scene name='48/488500/Cv/5'>active site</scene> contains Mg<sup>+2</sup> ions which are essensial for DUTP activity. The <scene name='48/488500/Cv/6'>Mg+2 ions are hexacoordinated to acidic residues and water molecules</scene>.<ref>PMID:15364583</ref> Water molecules are labeled Wa.


[[1dud]] – EcDUTP + dUDP<br />
==3D structures of dUTPase==
[[2hrm]] - EcDUTP + dUTP derivative<br />
[[dUTPase 3D structures]]
[[1seh]] - EcDUTP + dUMP<br />
[[3f4f]] - yDUTP + dUMP<br />
[[1dut]] – DUTP + Mg – Feline immunodeficiency virus<br />
[[1ogk]] – TcDUTP + dUTP<br />
[[1smc]] - MtDUTP + dUTP<br />
[[1vyq]] - PfDUTP + inhibitor – ''Plasmodium falciparum''<br />
[[2y8c]] - PfDUTP + trityl ligand<br />
[[2bsy]], [[2we0]] - EbvDUTP + dUMP – Epstein-Barr virus<br />
[[2we1]], [[2we2]] - EbvDUTP (mutant) + dUMP<br />
[[2ol1]] - VvDUTP + dUMP<br />
[[2y1t]] - BsDUTP + dUDP<br />
[[2yb0]] - LmDUTP + dU – ''Leishmania major''<br />
[[3tq5]], [[3trl]], [[3trn]], [[3ts6]], [[3tsl]], [[3tta]] - MPmvDUTP catalytic domain (mutant) + dUMP<br />


'''DUTP ternary complexes'''
</StructureSection>


[[1duc]] – EvDUPT + Sr + dUTP<br />
== References ==
[[1six]], [[1sjn]], [[2py4]] – MtDUTP + Mg + dUTP derivative<br />
<references/>
[[3h6d]], [[3hza]], [[3i93]] - MtDUTP (mutant) + Mg + dUTP derivative<br />
[[Category:Topic Page]]
[[3loj]] - MtDUTP (mutant) + Mg + Mn + dUTP derivative<br />
[[1rn8]] - EcDUTP + Mg + dUTP derivative<br />
[[1rnj]] - EcDUTP (mutant) + Mg + dUTP derivative<br />
[[1syl]] - EcDUTP (mutant) + Mg + dUTP<br />
[[2hr6]] - EcDUTP + Mn + dUDP<br />
[[1slh]] – MtDUTP + Mg + dUTP<br />
[[1sm8]] – MtDUTP + Cr + dUTP<br />
[[1snf]] - MtDUTP + Mg + dUMP<br />
[[1w2y]], [[2cic]] - DUTP + Mg + dUTP derivative – ''Campylobacter jejuni''<br />
[[2bt1]] - EbvDUTP + Mg + dUTP derivative<br />
[[2we3]] - EbvDUTP residues 1-256 + Mg + dUTP<br />
[[2d4n]] - MPmvDUTP residues 83-234 (mutant) + Mg + dUTP derivative<br />
[[3tp1]] - MPmvDUTP catalytic domain + Mg + dUTP derivative<br />
[[3tpw]], [[3tpn]], [[3tps]] - MPmvDUTP catalytic domain (mutant) + Mg + dUTP derivative<br />
[[3tpy]], [[3tq3]], [[3tq4]] - MPmvDUTP catalytic domain + Mg + dUMP + dUTP derivative<br />
[[2cje]] - LmDUTP + Mg + dUTP derivative<br />
[[2yay]] - LmDUTP + Ca + dUTP derivative<br />
[[2yaz]] - LmDUTP + Mg + dUMP<br />
[[2oke]] - VvDUTP + Mg + dUTP derivative<br />
[[2ol0]] - VvDUTP + Mg + dUDP<br />
[[3c3i]] - PbcvDUTP (mutant) + Mg + dUDP – Paramecium bursaria chlorella virus<br />
[[3c2t]], [[3ca9]] - PbcvDUTP + Mg + dUDP<br />
[[2hqu]] - hDUTP + Mg + dUTP derivative – human<br />
[[3ara]], [[3arn]] - hDUTP + Mg + uracil derivative<br />
[[3p48]] - yDUTP + Mg + dUTP derivative<br />
[[2xy3]] - BsDUTP + Mg + dUTP derivative<br />

Latest revision as of 10:50, 27 June 2021


Function

Deoxyuridine 5’-triphosphate nucleotidohydrolase or Deoxyuridine triphosphatase or dUTP pyrophosphatase (DUTP) catalyzes the conversion of dUTP to dUMP and pyrophosphate (PPi). DUTP plays a key role in keeping significant amounts of dUTP from the DNA synthesis pathway.

Prokaryotic DUTP contains metal ion. [1]

Relevance

DUTP inhibitors are being tested as possible anti-bacterial agents targeting diseases like malaria, leishmaniasis, tuberculosis and trypanosomiasis.

Structural highlights

The contains Mg+2 ions which are essensial for DUTP activity. The .[2] Water molecules are labeled Wa.

3D structures of dUTPase

dUTPase 3D structures


dUTPase complex with dUTP analog and Mg+2 ions (green) (PDB entry 1w2y)

Drag the structure with the mouse to rotate

ReferencesReferences

  1. ↑ Vertessy BG, Toth J. Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases. Acc Chem Res. 2009 Jan 20;42(1):97-106. PMID:18837522 doi:10.1021/ar800114w
  2. ↑ Moroz OV, Harkiolaki M, Galperin MY, Vagin AA, Gonzalez-Pacanowska D, Wilson KS. The crystal structure of a complex of Campylobacter jejuni dUTPase with substrate analogue sheds light on the mechanism and suggests the "basic module" for dimeric d(C/U)TPases. J Mol Biol. 2004 Oct 1;342(5):1583-97. PMID:15364583 doi:10.1016/j.jmb.2004.07.050

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Michal Harel, Alexander Berchansky
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