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| {{STRUCTURE_1oe5| PDB=1oe5 | SCENE= }} | | {{STRUCTURE_1oe5| PDB=1oe5 | SCENE= }} |
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| '''XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE'''
| | ===XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12820976}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12820976 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12820976}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Single stranded]] | | [[Category: Single stranded]] |
| [[Category: Smug1]] | | [[Category: Smug1]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:43:54 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:58:36 2008'' |
