1oe4
From Proteopedia
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| - | [[Image:1oe4.gif|left|200px]] | + | [[Image:1oe4.gif|left|200px]] |
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| - | '''XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE''' | + | {{Structure |
| + | |PDB= 1oe4 |SIZE=350|CAPTION= <scene name='initialview01'>1oe4</scene>, resolution 2.00Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Ipa+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OE4 is a [ | + | 1OE4 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE4 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12820976 12820976] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
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[[Category: smug1]] | [[Category: smug1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:09:34 2008'' |
Revision as of 11:09, 20 March 2008
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| , resolution 2.00Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1OE4 is a Protein complex structure of sequences from Xenopus laevis. 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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