1sxj
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(New page: 200px<br /><applet load="1sxj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sxj, resolution 2.85Å" /> '''Crystal Structure of...)
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Revision as of 00:41, 21 November 2007
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Crystal Structure of the Eukaryotic Clamp Loader (Replication Factor C, RFC) Bound to the DNA Sliding Clamp (Proliferating Cell Nuclear Antigen, PCNA)
Overview
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.
About this Structure
1SXJ is a Protein complex structure of sequences from Saccharomyces cerevisiae with MG, ATG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
Structural analysis of a eukaryotic sliding DNA clamp-clamp loader complex., Bowman GD, O'Donnell M, Kuriyan J, Nature. 2004 Jun 17;429(6993):724-30. PMID:15201901
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