Structural analysis of a eukaryotic sliding DNA clamp–clamp loader complex
Gregory D. Bowman,
Mike O'Donnell and
John Kuriyan ()
Additional contact information
Gregory D. Bowman: University of California
Mike O'Donnell: The Rockefeller University
John Kuriyan: University of California
Nature, 2004, vol. 429, issue 6993, 724-730
Abstract:
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-γS 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.
Date: 2004
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:429:y:2004:i:6993:d:10.1038_nature02585
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DOI: 10.1038/nature02585
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