1SXJ
Crystal Structure of the Eukaryotic Clamp Loader (Replication Factor C, RFC) Bound to the DNA Sliding Clamp (Proliferating Cell Nuclear Antigen, PCNA)
Summary for 1SXJ
Entry DOI | 10.2210/pdb1sxj/pdb |
Related | 1PLQ |
Descriptor | Activator 1 95 kDa subunit, Activator 1 37 kDa subunit, Activator 1 40 kDa subunit, ... (9 entities in total) |
Functional Keywords | clamp loader, processivity clamp, dna sliding clamp, aaa+ atpase, dna polymerase, dna-binding protein, replication |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Cellular location | Nucleus (Probable): P38630 P40339 P38629 P40348 P38251 Nucleus: P15873 |
Total number of polymer chains | 8 |
Total formula weight | 309282.41 |
Authors | Bowman, G.D.,O'Donnell, M.,Kuriyan, J. (deposition date: 2004-03-30, release date: 2004-06-22, Last modification date: 2024-10-09) |
Primary citation | Bowman, G.D.,O'Donnell, M.,Kuriyan, J. Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex. Nature, 429:724-730, 2004 Cited by PubMed 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. PubMed: 15201901DOI: 10.1038/nature02585 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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