1oe5
From Proteopedia
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| - | [[Image:1oe5.gif|left|200px]]<br /> | + | [[Image:1oe5.gif|left|200px]]<br /><applet load="1oe5" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1oe5" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1oe5, resolution 2.30Å" /> | caption="1oe5, resolution 2.30Å" /> | ||
'''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== | ||
| - | 1OE5 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 URA, EPE, DUR, GOL and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 1OE5 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 URA, EPE, DUR, GOL and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Epe Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OE5 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: smug1]] | [[Category: smug1]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:35:13 2007'' |
Revision as of 15:25, 18 December 2007
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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
1OE5 is a Protein complex structure of sequences from Xenopus laevis with URA, EPE, DUR, 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
Page seeded by OCA on Tue Dec 18 17:35:13 2007
Categories: Protein complex | Xenopus laevis | Pearl, L.H. | Wibley, J.E.A. | DUR | EPE | GOL | IPA | URA | Dna glycosylase | Single stranded | Smug1
