Journal
NATURE
Volume 429, Issue 6993, Pages 724-730Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature02585
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Funding
- NIGMS NIH HHS [F32 GM066586, F32 GM066586-01, F32 GM066586-02] Funding Source: Medline
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Sliding clamps are ring-shaped proteins that encircle DNA and confer high processivity on DNA polymerases. Here we report the crystal structure of the five-protein clamp loader complex ( replication factor-C, RFC) of the yeast Saccharomyces cerevisiae, bound to the sliding clamp ( proliferating cell nuclear antigen, PCNA). Tight interfacial coordination of the ATP analogue ATP-gamma S by RFC results in a spiral arrangement of the ATPase domains of the clamp loader above the PCNA ring. Placement of a model for primed DNA within the central hole of PCNA reveals a striking correspondence between the RFC spiral and the grooves of the DNA double helix. This model, in which the clamp loader complex locks onto primed DNA in a screw-cap-like arrangement, provides a simple explanation for the process by which the engagement of primer-template junctions by the RFC: PCNA complex results in ATP hydrolysis and release of the sliding clamp on DNA.
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