1rrs: Difference between revisions

Revision as of 13:33, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1rrs.png

Template:STRUCTURE 1rrs

MutY adenine glycosylase in complex with DNA containing an abasic siteMutY adenine glycosylase in complex with DNA containing an abasic site

Template:ABSTRACT PUBMED 14961129

About this StructureAbout this Structure

1RRS is a Single protein structure of sequence from Geobacillus stearothermophilus. 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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OCA

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-'''MutY adenine glycosylase in complex with DNA containing an abasic site'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14961129}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14961129 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14961129}}
 ==About this Structure==
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 [[Category: Dna repair]]
 [[Category: Protein-dna complex]]
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