3FHG

Crystal structure of Sulfolobus solfataricus 8-oxoguanine DNA glycosylase (SsOgg)

Summary for 3FHG

• Entry DOI: 10.2210/pdb3fhg/pdb
• Related: 3FHF
• Descriptor: N-glycosylase/DNA lyase, GLYCEROL, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ogg, helix-hairpin-helix, glycosylase, 8-oxoguanine, 8-oxog, ssogg, dna damage, dna repair, glycosidase, hydrolase, lyase, multifunctional enzyme, nuclease
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 1
• Total formula weight: 25707.37

Authors

Faucher, F.,Doublie, S. (deposition date: 2008-12-09, release date: 2009-05-19, Last modification date: 2024-11-06)

Primary citation

Faucher, F.,Duclos, S.,Bandaru, V.,Wallace, S.S.,Doublie, S.
Crystal structures of two archaeal 8-oxoguanine DNA glycosylases provide structural insight into guanine/8-oxoguanine distinction.
Structure, 17:703-712, 2009

PubMed Abstract: Among the four DNA bases, guanine is particularly vulnerable to oxidative damage and the most common oxidative product, 7,8-dihydro-8-oxoguanine (8-oxoG), is the most prevalent lesion observed in DNA molecules. Fortunately, 8-oxoG is recognized and excised by the 8-oxoguanine DNA glycosylase (Ogg) of the base excision repair pathway. Ogg enzymes are divided into three separate families, namely, Ogg1, Ogg2, and archaeal GO glycosylase (AGOG). To date, structures of members of both Ogg1 and AGOG families are known but no structural information is available for members of Ogg2. Here we describe the first crystal structures of two archaeal Ogg2: Methanocaldococcus janischii Ogg and Sulfolobus solfataricus Ogg. A structural comparison with OGG1 and AGOG suggested that the C-terminal lysine of Ogg2 may play a key role in discriminating between guanine and 8-oxoG. This prediction was substantiated by measuring the glycosylase/lyase activity of a C-terminal deletion mutant of MjaOgg.

PubMed: 19446526
DOI: 10.1016/j.str.2009.03.007

Experimental method

X-RAY DIFFRACTION (1.9 Å)