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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 DOI10.2210/pdb1sxj/pdb
Related1PLQ
DescriptorActivator 1 95 kDa subunit, Activator 1 37 kDa subunit, Activator 1 40 kDa subunit, ... (9 entities in total)
Functional Keywordsclamp loader, processivity clamp, dna sliding clamp, aaa+ atpase, dna polymerase, dna-binding protein, replication
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Cellular locationNucleus (Probable): P38630 P40339 P38629 P40348 P38251
Nucleus: P15873
Total number of polymer chains8
Total formula weight309282.41
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 citationBowman, 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: 15201901
DOI: 10.1038/nature02585
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.85 Å)
Structure validation

226707

건을2024-10-30부터공개중

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