The Mechanism of ATP-Dependent Primer-Template Recognition by a Clamp Loader Complex

@article{Simonetta2009TheMO,
  title={The Mechanism of ATP-Dependent Primer-Template Recognition by a Clamp Loader Complex},
  author={Kyle R. Simonetta and Steven L. Kazmirski and Eric R. Goedken and Aaron J Cantor and Brian A. Kelch and Randall McNally and Steven N. Seyedin and Debora Lika Makino and Mike O'Donnell and John Kuriyan},
  journal={Cell},
  year={2009},
  volume={137},
  pages={659-671}
}
Clamp loaders load sliding clamps onto primer-template DNA. The structure of the E. coli clamp loader bound to DNA reveals the formation of an ATP-dependent spiral of ATPase domains that tracks only the template strand, allowing recognition of both RNA and DNA primers. Unlike hexameric helicases, in which DNA translocation requires distinct conformations of the ATPase domains, the clamp loader spiral is symmetric and is set up to trigger release upon DNA recognition. Specificity for primed DNA… CONTINUE READING
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