1vrl
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MutY adenine glycosylase in complex with DNA and soaked adenine free base
OverviewOverview
The genomes of aerobic organisms suffer chronic oxidation of guanine to, the genotoxic product 8-oxoguanine (oxoG). Replicative DNA polymerases, misread oxoG residues and insert adenine instead of cytosine opposite the, oxidized base. Both bases in the resulting A*oxoG mispair are mutagenic, lesions, and both must undergo base-specific replacement to restore the, original C*G pair. Doing so represents a formidable challenge to the DNA, repair machinery, because adenine makes up roughly 25% of the bases in, most genomes. The evolutionarily conserved enzyme adenine DNA glycosylase, (called MutY in bacteria and hMYH in humans) initiates repair of A*oxoG to, C*G by removing the inappropriately paired adenine base from the DNA, backbone. A central issue concerning MutY function is the mechanism by, which A*oxoG mispairs are targeted among the vast excess of A*T pairs., Here we report the use of disulphide crosslinking to obtain, high-resolution crystal structures of MutY-DNA lesion-recognition, complexes. These structures reveal the basis for recognizing both lesions, in the A*oxoG pair and for catalysing removal of the adenine base.
About this StructureAbout this Structure
1VRL is a Protein complex structure of sequences from Geobacillus stearothermophilus with CA, SF4 and ADE as ligands. This structure superseeds the now removed PDB entry 1RRT. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase., Fromme JC, Banerjee A, Huang SJ, Verdine GL, Nature. 2004 Feb 12;427(6975):652-6. PMID:14961129
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