Deoxyuridine 5'-triphosphate nucleotidohydrolase: Difference between revisions

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**[[2yb0]] - LmDUTP + dU – ''Leishmania major''<br />
**[[2yb0]] - LmDUTP + dU – ''Leishmania major''<br />
**[[3tq5]], [[3trl]], [[3trn]], [[3ts6]], [[3tsl]], [[3tta]] - MPmvDUTP catalytic domain (mutant) + dUMP<br />
**[[3tq5]], [[3trl]], [[3trn]], [[3ts6]], [[3tsl]], [[3tta]] - MPmvDUTP catalytic domain (mutant) + dUMP<br />
**[[4ooq]], [[2pc5]] – DUTP + 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 />


Line 70: Line 70:
**[[2hr6]] - EcDUTP + Mn + dUDP<br />  
**[[2hr6]] - EcDUTP + Mn + dUDP<br />  
**[[1slh]] – MtDUTP + Mg + dUDP<br />
**[[1slh]] – MtDUTP + Mg + dUDP<br />
**[[5ect]], [[5edd]] - MtDUTP (mutant) + Mg + dUTP derivative<br />
**[[1sm8]] – MtDUTP + Cr + dUTP<br />
**[[1sm8]] – MtDUTP + Cr + dUTP<br />
**[[1snf]] - MtDUTP + Mg + dUMP<br />
**[[1snf]] - MtDUTP + Mg + dUMP<br />
**[[1w2y]], [[2cic]] - DUTP + Mg + dUTP derivative – ''Campylobacter jejuni''<br />
**[[1w2y]], [[2cic]] - DUTP + Mg + dUTP derivative – ''Campylobacter jejuni''<br />
**[[5f9k]] - DUTP + Mg + dUTP derivative – slime mold<br />
**[[2bt1]] - EbvDUTP + Mg + dUTP derivative<br />
**[[2bt1]] - EbvDUTP + Mg + dUTP derivative<br />
**[[2we3]] - EbvDUTP residues 1-256 + Mg + dUTP<br />
**[[2we3]] - EbvDUTP residues 1-256 + Mg + dUTP<br />
Line 92: Line 94:
**[[3p48]] - yDUTP + Mg + dUTP derivative<br />
**[[3p48]] - yDUTP + Mg + dUTP derivative<br />
**[[2xy3]] - BsDUTP + Mg + dUTP derivative<br />
**[[2xy3]] - BsDUTP + Mg + dUTP derivative<br />
**[[4oop]] - AtDUTP + Mg + dUTP derivative<br />
**[[4aoo]], [[4apz]], [[4aoz]] - BsDUTP + Mg + PPi + uridine<br />
**[[4aoo]], [[4apz]], [[4aoz]] - BsDUTP + Mg + PPi + uridine<br />
}}
}}

Revision as of 09:58, 18 April 2017


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)

Drag the structure with the mouse to rotate

3D structures of dUTPase3D structures of dUTPase

Updated on 18-April-2017

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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