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1oe6

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[[Image:1oe6.gif|left|200px]]<br />
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[[Image:1oe6.gif|left|200px]]<br /><applet load="1oe6" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1oe6" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1oe6, resolution 2.65&Aring;" />
caption="1oe6, resolution 2.65&Aring;" />
'''XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE'''<br />
'''XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE'''<br />
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==About this Structure==
==About this Structure==
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1OE6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with HMU, GOL and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OE6 OCA].
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1OE6 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with HMU, GOL and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Ipa Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OE6 OCA].
==Reference==
==Reference==
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[[Category: smug1]]
[[Category: smug1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:51:32 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:35:15 2007''

Revision as of 15:25, 18 December 2007


1oe6, resolution 2.65Å

Drag the structure with the mouse to rotate

XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE

Overview

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, base-excision products. This structure indicates a more invasive, interaction with dsDNA than observed with other UDGs and reveals an, elegant water displacement/replacement mechanism that allows SMUG1 to, exclude thymine from its active site while accepting HmU.

About this Structure

1OE6 is a Protein complex structure of sequences from Xenopus laevis with HMU, GOL and IPA as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

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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