Deoxyuridine 5'-triphosphate nucleotidohydrolase: Difference between revisions

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**[[1q5u]] - hDUTP – human<br />
**[[1q5u]] - hDUTP – human<br />
**[[4lhr]] - DUTP – ''Burkholderia thailandensis''<br />
**[[4lhr]] - DUTP – ''Burkholderia thailandensis''<br />
**[[3h6x]] - DUTP – ''Streptococcus mutans''<br />
**[[5myf]] - SaDUTP – ''Staphylococcus aureus''<br />
**[[5myi]] - SaDUTP (mutant)<br />


*DUTP binary complexes
*DUTP binary complexes
Line 47: Line 50:
**[[1smc]] - MtDUTP + dUTP<br />
**[[1smc]] - MtDUTP + dUTP<br />
**[[4gcy]] - MtDUTP (mutant) + dUTP<br />
**[[4gcy]] - MtDUTP (mutant) + dUTP<br />
**[[4a6a]] - MtDUTP (mutant) + dTTP<br />
**[[1vyq]], [[3t60]], [[3t64]], [[3t6y]], [[3t70]] - PfDUTP + uridine derivative inhibitor – ''Plasmodium falciparum''<br />
**[[1vyq]], [[3t60]], [[3t64]], [[3t6y]], [[3t70]] - PfDUTP + uridine derivative inhibitor – ''Plasmodium falciparum''<br />
**[[2y8c]] - PfDUTP + trityl ligand<br />
**[[2y8c]] - PfDUTP + trityl ligand<br />
Line 58: Line 62:
**[[4ooq]], [[2pc5]] – AtDUTP + Mg – ''Arabidopsis thaliana''<br />
**[[4ooq]], [[2pc5]] – AtDUTP + Mg – ''Arabidopsis thaliana''<br />
**[[4mz5]], [[4mz6]] – hDUTP + importin subunit α-1<br />
**[[4mz5]], [[4mz6]] – hDUTP + importin subunit α-1<br />
**[[5h4j]] - hDUTP + inhibitor<br />
**[[3zf0]], [[3zf1]], [[3zf2]], [[3zf3]], [[3zf4]], [[3zf5]], [[3zf6]], [[5cct]], [[5nyz]], [[5nz2]] - SpDUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage 80α<br />
**[[5cco]] - SpDUTP + dUMP  <br />
**[[4gv8]] - DUTP + dUTP derivative – ''Staphylococcus'' phage 11<br />
**[[4wrk]] - DUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage φ11<br />
**[[5myd]] - DUTP + dUTP derivative – ''Staphylococcus'' <br />


*DUTP ternary complexes
*DUTP ternary complexes

Revision as of 09:40, 24 April 2018


Function

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.

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.

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

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3D structures of dUTPase3D structures of dUTPase

Updated on 24-April-2018

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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky
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