Structure
The crystallographic structure of a Cdc6p/Orc1-related protein from Pyrobaculum aerophilum (see Pyrobaculum) has been solved and three structural domains have been identified. Domain I and II form the ATP binding/hydrolysis site and are similar to other AAA+ ATPases. Domain III is structurally related to a winged-helix domain, thus may interact with origin DNA. From studies with E. coli γ clamp loading complex, it was suggested that domain III mediates protein-protein interactions with other AAA+ ATPases in the pre-RC, thus suggesting that the Cdc6p builds a homodimer in its native form. The domains I and II form a cashew-shaped molecule that bind ATP in the cleft and additionally build the sensor motif for ATP/ADP recognition. These domains are also thought to mediate subsequent conformational changes. Nevertheless, the exact functional roles of these domains remain unclear.
Read more about this topic: CDC6
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