Deoxyuridine 5'-triphosphate nucleotidohydrolase
From Proteopedia
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| - | <StructureSection load='1w2y' size='350' side='right' caption='dUTPase | + | <StructureSection load='1w2y' size='350' side='right' caption='dUTPase complex with dUTP analog (stick model) and Mg+2 ions (green) (PDB entry [[1w2y]])' scene=''> |
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DUTP inhibitors are being tested as possible anti-bacterial agents targeting diseases like malaria, leishmaniasis, tuberculosis and trypanosomiasis. | DUTP inhibitors are being tested as possible anti-bacterial agents targeting diseases like malaria, leishmaniasis, tuberculosis and trypanosomiasis. | ||
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| + | == Structural highlights == | ||
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| + | 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> | ||
</StructureSection> | </StructureSection> | ||
==3D structures of dUTPase== | ==3D structures of dUTPase== | ||
Revision as of 11:58, 23 December 2015
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3D structures of dUTPase
Updated on 23-December-2015
References
- ↑ 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
