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- Title
Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex.
- Authors
Bowman, Gregory D; O'Donnell, Mike; Kuriyan, John
- Abstract
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-gammaS 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.
- Publication
Nature, 2004, Vol 429, Issue 6993, p724
- ISSN
1476-4687
- Publication type
Journal Article
- DOI
10.1038/nature02585