1oe5

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Revision as of 19:13, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1oe5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oe5, resolution 2.30Å" /> '''XENOPUS SMUG1, AN A...)
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File:1oe5.gif


1oe5, resolution 2.30Å

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XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE

OverviewOverview

Cytosine deamination is a major promutagenic process, generating G:U, mismatches that can cause transition mutations if not repaired. Uracil is, also introduced into DNA via nonmutagenic incorporation of dUTP during, replication. In bacteria, uracil is excised by uracil-DNA glycosylases, (UDG) related to E. coli UNG, and UNG homologs are found in mammals and, viruses. Ung knockout mice display no increase in mutation frequency due, to a second UDG activity, SMUG1, which is specialized for antimutational, uracil excision in mammalian cells. Remarkably, SMUG1 also excises the, oxidation-damage product 5-hydroxymethyluracil (HmU), but like UNG is, inactive against thymine (5-methyluracil), a chemical substructure of HmU., We have solved the crystal structure of SMUG1 complexed with DNA and, ... [(full description)]

About this StructureAbout this Structure

1OE5 is a [Protein complex] structure of sequences from [Xenopus laevis] with URA, EPE, DUR, GOL and IPA as [ligands]. Full crystallographic information is available from [OCA].

ReferenceReference

Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1., Wibley JE, Waters TR, Haushalter K, Verdine GL, Pearl LH, Mol Cell. 2003 Jun;11(6):1647-59. PMID:12820976

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