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3I0X

Crystal structure of Clostridium acetobutylicum 8-oxoguanine glycosylase/lyase in complex with dsDNA containing adenine opposite to 8-oxoG

Summary for 3I0X
Entry DOI10.2210/pdb3i0x/pdb
Related3I0W
Descriptor8-oxoguanine-DNA-glycosylase, 5'-D(*AP*TP*CP*CP*AP*(8OG)P*GP*TP*CP*TP*AP*CP*C)-3', 5'-D(*GP*GP*TP*AP*GP*AP*CP*AP*TP*GP*GP*A)-3', ... (5 entities in total)
Functional Keywordsogg, cacogg, dna, 8-oxog, 8oxog, glycosylase, adenine, hydrolase, lyase-dna complex, lyase/dna
Biological sourceClostridium acetobutylicum
More
Total number of polymer chains3
Total formula weight42054.33
Authors
Faucher, F.,Doublie, S. (deposition date: 2009-06-25, release date: 2009-09-29, Last modification date: 2024-02-21)
Primary citationFaucher, F.,Wallace, S.S.,Doublie, S.
Structural basis for the lack of opposite base specificity of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase.
Dna Repair, 8:1283-1289, 2009
Cited by
PubMed Abstract: 7,8-Dihydro-8-oxoguanine (8-oxoG) is the major oxidative product of guanine and the most prevalent base lesion observed in DNA molecules. Because 8-oxoG has the capability to form a Hoogsteen pair with adenine (8-oxoG:A) in addition to a normal Watson-Crick pair with cytosine (8-oxoG:C), this lesion can lead to a G:C-->T:A transversion after replication. However, 8-oxoG is recognized and excised by the 8-oxoguanine DNA glycosylase (Ogg) of the base excision repair pathway. Members of the Ogg1 family usually display a strong preference for a C opposite the lesion. In contrast, the atypical Ogg1 from Clostridium actetobutylicum (CacOgg) can excise 8-oxoG when paired with either one of the four bases, albeit with a preference for C and A. Here we describe the first high-resolution crystal structures of CacOgg in complex with duplex DNA containing the 8-oxoG lesion paired to cytosine and to adenine. A structural comparison with human OGG1 provides a rationale for the lack of opposite base specificity displayed by the bacterial Ogg.
PubMed: 19747886
DOI: 10.1016/j.dnarep.2009.08.002
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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数据于2024-11-06公开中

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