1jql
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(New page: 200px<br /><applet load="1jql" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jql, resolution 2.5Å" /> '''Mechanism of Processi...)
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Revision as of 16:21, 20 November 2007
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Mechanism of Processivity Clamp Opening by the Delta Subunit Wrench of the Clamp Loader Complex of E. coli DNA Polymerase III: Structure of beta-delta (1-140)
Overview
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.
About this Structure
1JQL is a Protein complex structure of sequences from Escherichia coli. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
Reference
Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III., Jeruzalmi D, Yurieva O, Zhao Y, Young M, Stewart J, Hingorani M, O'Donnell M, Kuriyan J, Cell. 2001 Aug 24;106(4):417-28. PMID:11525728
Page seeded by OCA on Tue Nov 20 18:29:12 2007
