3ehw

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Template:STRUCTURE 3ehw

Contents

Human dUTPase in complex with alpha,beta-imido-dUTP and Mg2+: visualization of the full-length C-termini in all monomers and suggestion for an additional metal ion binding site

Template:ABSTRACT PUBMED 19302784

Function

[DUT_HUMAN] This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.[1]

About this Structure

3ehw is a 6 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Takacs E, Barabas O, Petoukhov MV, Svergun DI, Vertessy BG. Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers. FEBS Lett. 2009 Mar 4;583(5):865-71. Epub 2009 Feb 11. PMID:19302784 doi:10.1016/j.febslet.2009.02.011
  • Mol CD, Harris JM, McIntosh EM, Tainer JA. Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. Structure. 1996 Sep 15;4(9):1077-92. PMID:8805593
  • Varga B, Barabas O, Kovari J, Toth J, Hunyadi-Gulyas E, Klement E, Medzihradszky KF, Tolgyesi F, Fidy J, Vertessy BG. Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase. FEBS Lett. 2007 Oct 2;581(24):4783-8. Epub 2007 Sep 12. PMID:17880943 doi:10.1016/j.febslet.2007.09.005
  1. ↑ Mol CD, Harris JM, McIntosh EM, Tainer JA. Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. Structure. 1996 Sep 15;4(9):1077-92. PMID:8805593

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