1rrs
From Proteopedia
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MutY adenine glycosylase in complex with DNA containing an abasic site
Overview
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 Structure
1RRS is a Single protein structure of sequence from Geobacillus stearothermophilus with CA and SF4 as ligands. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sat Nov 24 23:09:48 2007
