1xqo
From Proteopedia
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Crystal structure of native Pa-AGOG, 8-oxoguanine DNA glycosylase from Pyrobaculum aerophilum
Overview
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.
About this Structure
1XQO is a Single protein structure of sequence from Pyrobaculum aerophilum. Full crystallographic information is available from OCA.
Reference
A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure., Lingaraju GM, Sartori AA, Kostrewa D, Prota AE, Jiricny J, Winkler FK, Structure. 2005 Jan;13(1):87-98. PMID:15642264
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