1oe5
From Proteopedia
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'''XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE''' | '''XENOPUS SMUG1, AN ANTI-MUTATOR URACIL-DNA GLYCOSYLASE''' | ||
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[[Category: Pearl, L H.]] | [[Category: Pearl, L H.]] | ||
[[Category: Wibley, J E.A.]] | [[Category: Wibley, J E.A.]] | ||
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| - | [[Category: | + | [[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 | + | |
Revision as of 00:43, 3 May 2008
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. 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 Sat May 3 03:43:54 2008
