1JQJ

Mechanism of Processivity Clamp Opening by the Delta Subunit Wrench of the Clamp Loader Complex of E. coli DNA Polymerase III: Structure of the beta-delta complex

Summary for 1JQJ

• Entry DOI: 10.2210/pdb1jqj/pdb
• Related: 1JQL 1JR3 1a5t 2pol
• Descriptor: DNA polymerase III, beta chain, DNA polymerase III, delta subunit (2 entities in total)
• Functional Keywords: dna polymerase, processivity clamp, clamp loader, dna replication, aaa+ atpase, transferase
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm : P0A988
• Total number of polymer chains: 4
• Total formula weight: 158583.85

Authors

Jeruzalmi, D.,Yurieva, O.,Zhao, Y.,Young, M.,Stewart, J.,Hingorani, M.,O'Donnell, M.,Kuriyan, J. (deposition date: 2001-08-07, release date: 2001-11-07, Last modification date: 2024-02-07)

Primary citation

Jeruzalmi, D.,Yurieva, O.,Zhao, Y.,Young, M.,Stewart, J.,Hingorani, M.,O'Donnell, M.,Kuriyan, J.
Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III.
Cell(Cambridge,Mass.), 106:417-428, 2001

PubMed Abstract: The dimeric ring-shaped sliding clamp of E. coli DNA polymerase III (beta subunit, homolog of eukaryotic PCNA) is loaded onto DNA by the clamp loader gamma complex (homolog of eukaryotic Replication Factor C, RFC). The delta subunit of the gamma complex binds to the beta ring and opens it. The crystal structure of a beta:delta complex shows that delta, which is structurally related to the delta' and gamma subunits of the gamma complex, is a molecular wrench that induces or traps a conformational change in beta such that one of its dimer interfaces is destabilized. Structural comparisons and molecular dynamics simulations suggest a spring-loaded mechanism in which the beta ring opens spontaneously once a dimer interface is perturbed by the delta wrench.

PubMed: 11525728
DOI: 10.1016/S0092-8674(01)00462-7

Experimental method

X-RAY DIFFRACTION (2.9 Å)