Deoxyuridine 5'-triphosphate nucleotidohydrolase: Difference between revisions
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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. | 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. | ||
==3D structures of dUTPase== | |||
[[dUTPase 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
==3D structures of dUTPase== | ==3D structures of dUTPase== | ||
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*DUTP | *DUTP | ||
**[[1q5u]] - hDUTP – human<br /> | |||
**[[1dup]], [[1eu5]], [[1euw]] – EcDUTP – ''Escherichia coli''<br /> | **[[1dup]], [[1eu5]], [[1euw]] – EcDUTP – ''Escherichia coli''<br /> | ||
**[[1dun]] – EvDUTP – Equine infectious anemia virus<br /> | **[[1dun]] – EvDUTP – Equine infectious anemia virus<br /> | ||
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**[[2xx6]] - BsDUTP – ''Bacillus subtilis''<br /> | **[[2xx6]] - BsDUTP – ''Bacillus subtilis''<br /> | ||
**[[3tqz]] - DUTP – ''Coxiella burnetii''<br /> | **[[3tqz]] - DUTP – ''Coxiella burnetii''<br /> | ||
**[[4lhr]] - DUTP – ''Burkholderia thailandensis''<br /> | **[[4lhr]] - DUTP – ''Burkholderia thailandensis''<br /> | ||
**[[3h6x]] - DUTP – ''Streptococcus mutans''<br /> | **[[3h6x]] - DUTP – ''Streptococcus mutans''<br /> | ||
**[[5myf]] - SaDUTP – ''Staphylococcus aureus''<br /> | **[[5myf]] - SaDUTP – ''Staphylococcus aureus''<br /> | ||
**[[5myi]] - SaDUTP (mutant)<br /> | **[[5myi]] - SaDUTP (mutant)<br /> | ||
**[[6mai]] - LpDUTP – ''Legionella pneumophila''<br /> | |||
*DUTP binary complexes | *DUTP binary complexes | ||
**[[4mz5]], [[4mz6]] – hDUTP + importin subunit α-1<br /> | |||
**[[5h4j]] - hDUTP + inhibitor<br /> | |||
**[[1dud]] – EcDUTP + dUDP<br /> | **[[1dud]] – EcDUTP + dUDP<br /> | ||
**[[2hrm]] - EcDUTP + dUTP derivative<br /> | **[[2hrm]] - EcDUTP + dUTP derivative<br /> | ||
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**[[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]] – AtDUTP + Mg – ''Arabidopsis thaliana''<br /> | **[[4ooq]], [[2pc5]] – AtDUTP + Mg – ''Arabidopsis thaliana''<br /> | ||
**[[3zf0]], [[3zf1]], [[3zf2]], [[3zf3]], [[3zf4]], [[3zf5]], [[3zf6]], [[5cct]], [[5nyz]], [[5nz2]] - SpDUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage 80α<br /> | **[[3zf0]], [[3zf1]], [[3zf2]], [[3zf3]], [[3zf4]], [[3zf5]], [[3zf6]], [[5cct]], [[5nyz]], [[5nz2]] - SpDUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage 80α<br /> | ||
**[[5cco]] - SpDUTP + dUMP <br /> | **[[5cco]] - SpDUTP + dUMP <br /> | ||
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**[[4wrk]] - DUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage φ11<br /> | **[[4wrk]] - DUTP (mutant) + dUTP derivative – ''Staphylococcus'' phage φ11<br /> | ||
**[[5myd]] - DUTP + dUTP derivative – ''Staphylococcus'' <br /> | **[[5myd]] - DUTP + dUTP derivative – ''Staphylococcus'' <br /> | ||
**[[6mao]] - LpDUTP + dUMP <br /> | |||
*DUTP ternary complexes | *DUTP ternary complexes | ||
Revision as of 11:56, 5 June 2019
FunctionDeoxyuridine 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] RelevanceDUTP inhibitors are being tested as possible anti-bacterial agents targeting diseases like malaria, leishmaniasis, tuberculosis and trypanosomiasis. Structural highlightsThe contains Mg+2 ions which are essensial for DUTP activity. The .[2] Water molecules are labeled Wa. 3D structures of dUTPase
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3D structures of dUTPase3D structures of dUTPase
Updated on 05-June-2019
ReferencesReferences
- ↑ 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
- ↑ 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