Access
To read this story in full you will need to login or make a payment (see right).
Article
Nature 429, 724-730 (17 June 2004) | doi:10.1038/nature02585; Received 27 February 2004; Accepted 20 April 2004
Open Innovation Challenges
-
Direct Molecular Detection of Proteins and Nucleic Acids
This Challenge is looking for novel approaches to protein and nucleic acid detection. This is an Id...
-
Methods of Modeling Adaptation in Populations
The analysis of adaptation with a population is a frequently encountered computational modeling scen...
nature jobs
Faculty Position - Center for Viral Oncology
- University of Kansas Medical Center
- Kansas City, KS
Copy Editor
- Indegene Lifesystems Pvt. Ltd
- Bengaluru 560 071 India
Structural analysis of a eukaryotic sliding DNA clamp–clamp loader complex
Gregory D. Bowman1,2, Mike O'Donnell3 & John Kuriyan1,2
- Howard Hughes Medical Institute, Department of Molecular and Cell Biology and Department of Chemistry, University of California, Berkeley, California 94720, USA
- Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA
- Laboratory of DNA Replication, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021, USA
Correspondence to: John Kuriyan1,2 Email: kuriyan@berkeley.edu
The coordinates and structure factors have been deposited in the Protein Data Bank (accession code 1SXJ).
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-
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.
- Howard Hughes Medical Institute, Department of Molecular and Cell Biology and Department of Chemistry, University of California, Berkeley, California 94720, USA
- Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA
- Laboratory of DNA Replication, Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021, USA
Correspondence to: John Kuriyan1,2 Email: kuriyan@berkeley.edu
The coordinates and structure factors have been deposited in the Protein Data Bank (accession code 1SXJ).
To read this story in full you will need to login or make a payment (see right).
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
NEWS AND VIEWS
'Screw-cap' clamp loader proteins that threadNature Structural & Molecular Biology News and Views (01 Jul 2004)
Molecular biology The loader of the ringsNature News and Views (17 Jun 2004)
See all 5 matches for News And ViewsRESEARCH
The clamp-loading complex for processive DNA replicationNature Structural & Molecular Biology Article (01 Jul 2004)
Mapping the interaction of DNA with the Escherichia coli DNA polymerase clamp loader complexNature Structural & Molecular Biology Article (01 Feb 2005)
See all 43 matches for Research
