title: Clamp loader structure predicts the architecture of DNA polymerase III holoenzyme and RFC.
abstract: Recent determinations of the crystal structure of the Escherichia coli gamma complex and delta-beta assembly have shed light on the bacterial clamp loading reaction. In this review, we discuss the structures of delta-beta and the gamma(3)deltadelta' complex and its mechanism of action as a clamp loader of the E. coli beta sliding clamp. We also expand upon the implications of the structural findings to the structure and function of the eukaryotic clamp loader, RFC, and the structure of E. coli DNA polymerase III holoenzyme.
authors.affiliation: The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. odonnel@mail.rockefeller.edu
authors.forename: M
authors.initials: M
authors.lastname: O'Donnell
authors.forename: D
authors.initials: D
authors.lastname: Jeruzalmi
authors.forename: J
authors.initials: J
authors.lastname: Kuriyan
mesh_terms: D000818:Animals; D018360:Crystallography, X-Ray; D004258:DNA Polymerase III / Q000737:chemistry*; D004926:Escherichia coli / Q000201:enzymology; D005057:Eukaryotic Cells; D020035:Holoenzymes / Q000737:chemistry; D006801:Humans; D017434:Protein Structure, Tertiary
chemical_list: D020035:Holoenzymes; D004258:DNA Polymerase III