3F10

Crystal structure of Clostridium Acetobutylicum 8-oxoguanine DNA glycosylase in complex with 8-oxoguanosine

Summary for 3F10

• Entry DOI: 10.2210/pdb3f10/pdb
• Related: 3F0Z
• Descriptor: 8-oxoguanine-DNA-glycosylase, 2'-DEOXY-8-OXOGUANOSINE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: 8oxog, guanine, 8oxoguanine, ogg, glycosylase, 8-oxoguanine, hydrolase, lyase
• Biological source: Clostridium acetobutylicum
• Total number of polymer chains: 1
• Total formula weight: 34872.85

Authors

Faucher, F.,Doublie, S. (deposition date: 2008-10-27, release date: 2009-04-07, Last modification date: 2023-12-27)

Primary citation

Faucher, F.,Robey-Bond, S.M.,Wallace, S.S.,Doublie, S.
Structural characterization of Clostridium acetobutylicum 8-oxoguanine DNA glycosylase in its apo form and in complex with 8-oxodeoxyguanosine.
J.Mol.Biol., 387:669-679, 2009

PubMed Abstract: DNA is subject to a multitude of oxidative damages generated by oxidizing agents from metabolism and exogenous sources and by ionizing radiation. Guanine is particularly vulnerable to oxidation, and the most common oxidative product 8-oxoguanine (8-oxoG) is the most prevalent lesion observed in DNA molecules. 8-OxoG can form a normal Watson-Crick pair with cytosine (8-oxoG:C), but it can also form a stable Hoogsteen pair with adenine (8-oxoG:A), leading to a G:C-->T:A transversion after replication. Fortunately, 8-oxoG is recognized and excised by either of two DNA glycosylases of the base excision repair pathway: formamidopyrimidine-DNA glycosylase and 8-oxoguanine DNA glycosylase (Ogg). While Clostridium acetobutylicum Ogg (CacOgg) DNA glycosylase can specifically recognize and remove 8-oxoG, it displays little preference for the base opposite the lesion, which is unusual for a member of the Ogg1 family. This work describes the crystal structures of CacOgg in its apo form and in complex with 8-oxo-2'-deoxyguanosine. A structural comparison between the apo form and the liganded form of the enzyme reveals a structural reorganization of the C-terminal domain upon binding of 8-oxoG, similar to that reported for human OGG1. A structural comparison of CacOgg with human OGG1, in complex with 8-oxoG containing DNA, provides a structural rationale for the lack of opposite base specificity displayed by CacOgg.

PubMed: 19361427
DOI: 10.1016/j.jmb.2009.01.067

Experimental method

X-RAY DIFFRACTION (2.3 Å)