1oe6: Difference between revisions
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[[Image:1oe6.gif|left|200px]]<br /><applet load="1oe6" size=" | [[Image:1oe6.gif|left|200px]]<br /><applet load="1oe6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1oe6, resolution 2.65Å" /> | caption="1oe6, resolution 2.65Å" /> | ||
'''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== | ||
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:// | 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 <scene name='pdbligand=HMU:'>HMU</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=IPA:'>IPA</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: smug1]] | [[Category: smug1]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:56:52 2008'' | ||
Revision as of 10:56, 3 February 2008
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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, 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 StructureAbout this Structure
1OE6 is a Protein complex structure of sequences from Xenopus laevis with , and as ligands. Known structural/functional Site: . 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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