Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III

David Jeruzalmi, Olga Yurieva, Yanxiang Zhao, Matthew Young, Jelena Stewart, Manju Hingorani, Mike O'Donnell, John Kuriyan

Research output: Journal article publicationJournal articleAcademic researchpeer-review

205 Citations (Scopus)


The dimeric ring-shaped sliding clamp of E. coli DNA polymerase III (β subunit, homolog of eukaryotic PCNA) is loaded onto DNA by the clamp loader γ complex (homolog of eukaryotic Replication Factor C, RFC). The δ subunit of the γ complex binds to the β ring and opens it. The crystal structure of a β:δ complex shows that δ, which is structurally related to the δ′ and γ subunits of the γ complex, is a molecular wrench that induces or traps a conformational change in β such that one of its dimer interfaces is destabilized. Structural comparisons and molecular dynamics simulations suggest a spring-loaded mechanism in which the β ring opens spontaneously once a dimer interface is perturbed by the δ wrench.
Original languageEnglish
Pages (from-to)417-428
Number of pages12
Issue number4
Publication statusPublished - 24 Aug 2001
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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