3I0X
Crystal structure of Clostridium acetobutylicum 8-oxoguanine glycosylase/lyase in complex with dsDNA containing adenine opposite to 8-oxoG
Summary for 3I0X
Entry DOI | 10.2210/pdb3i0x/pdb |
Related | 3I0W |
Descriptor | 8-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 Keywords | ogg, cacogg, dna, 8-oxog, 8oxog, glycosylase, adenine, hydrolase, lyase-dna complex, lyase/dna |
Biological source | Clostridium acetobutylicum More |
Total number of polymer chains | 3 |
Total formula weight | 42054.33 |
Authors | Faucher, F.,Doublie, S. (deposition date: 2009-06-25, release date: 2009-09-29, Last modification date: 2024-02-21) |
Primary citation | Faucher, 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: 19747886DOI: 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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