Deoxyuridine 5'-triphosphate nucleotidohydrolase: Difference between revisions

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<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'>
<StructureSection load='1w2y' size='450' side='right' caption='dUTPase complex with dUTP analog and Mg+2 ions (green) (PDB entry [[1w2y]])' scene='48/488500/Cv/1'>


== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==


The active site contains Mg<sup>+2</sup> ions which are essensial for DUTP activity. The Mg<sup>+2</sup> ions are hexacordinated to acidic residues and water molecules.<ref>PMID:15364583</ref>
The <scene name='48/488500/Cv/3'>active site</scene> contains Mg<sup>+2</sup> ions which are essensial for DUTP activity. The Mg<sup>+2</sup> ions are hexacordinated to acidic residues and water molecules.<ref>PMID:15364583</ref>
</StructureSection>
</StructureSection>
==3D structures of dUTPase==
==3D structures of dUTPase==

Revision as of 13:35, 29 December 2015


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 Mg+2 ions are hexacordinated to acidic residues and water molecules.[2]

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 29-December-2015

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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