title: Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III.
abstract: The crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III has been determined. Three consecutive domains in the structure are arranged in a C-shaped architecture. The N-terminal domain contains a nonfunctional nucleotide binding site. The catalytic component of the clamp-loader complex is the gamma subunit, which is homologous to delta'. A sequence-structure alignment suggests that nucleotides bind to gamma at an interdomain interface within the inner surface of the "C." The alignment is extended to other clamp-loader complexes and to the RuvB family of DNA helicases, and suggests that each of these is assembled from C-shaped components that can open and close the jaws of the "C" in response to ATP binding and hydrolysis.
authors.affiliation: The Rockefeller University, New York, New York 10021, USA.
authors.forename: B
authors.initials: B
authors.lastname: Guenther
authors.forename: R
authors.initials: R
authors.lastname: Onrust
authors.forename: A
authors.initials: A
authors.lastname: Sali
authors.forename: M
authors.initials: M
authors.lastname: O'Donnell
authors.forename: J
authors.initials: J
authors.lastname: Kuriyan
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D004258:DNA Polymerase III / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D006868:Hydrolysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010710:Phosphates / Q000378:metabolism; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D010710:Phosphates; D000255:Adenosine Triphosphate; D004258:DNA Polymerase III