1XQP

Crystal structure of 8-oxoguanosine complexed Pa-AGOG, 8-oxoguanine DNA glycosylase from Pyrobaculum aerophilum

Summary for 1XQP

• Entry DOI: 10.2210/pdb1xqp/pdb
• Related: 1XQO
• Descriptor: 8-oxoguanine DNA glycosylase, 2'-DEOXY-8-OXOGUANOSINE (3 entities in total)
• Functional Keywords: helix-hairpin-helix, 8-oxoguanine dna glycosylase, archaea, p.aerophilum, pa-agog-8-oxoguanosine complex, dna repair, lyase
• Biological source: Pyrobaculum aerophilum
• Total number of polymer chains: 1
• Total formula weight: 30077.93

Authors

Lingaraju, G.M.,Sartori, A.A.,Kostrewa, D.,Prota, A.E.,Jiricny, J.,Winkler, F.K. (deposition date: 2004-10-13, release date: 2004-11-16, Last modification date: 2024-10-30)

Primary citation

Lingaraju, G.M.,Sartori, A.A.,Kostrewa, D.,Prota, A.E.,Jiricny, J.,Winkler, F.K.
A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure
Structure, 13:87-98, 2005

PubMed Abstract: Studies of DNA base excision repair (BER) pathways in the hyperthermophilic crenarchaeon Pyrobaculum aerophilum identified an 8-oxoguanine-DNA glycosylase, Pa-AGOG (archaeal GO glycosylase), with distinct functional characteristics. Here, we describe its crystal structure and that of its complex with 8-oxoguanosine at 1.0 and 1.7 A resolution, respectively. Characteristic structural features are identified that confirm Pa-AGOG to be the founding member of a functional class within the helix-hairpin-helix (HhH) superfamily of DNA repair enzymes. Its hairpin structure differs substantially from that of other proteins containing an HhH motif, and we predict that it interacts with the DNA backbone in a distinct manner. Furthermore, the mode of 8-oxoguanine recognition, which involves several hydrogen-bonding and pi-stacking interactions, is unlike that observed in human OGG1, the prototypic 8-oxoguanine HhH-type DNA glycosylase. Despite these differences, the predicted kinked conformation of bound DNA and the catalytic mechanism are likely to resemble those of human OGG1.

PubMed: 15642264
DOI: 10.1016/j.str.2004.10.011

Experimental method

X-RAY DIFFRACTION (1.69 Å)