PMID:9363942

Citation	Guenther, B, Onrust, R, Sali, A, O'Donnell, M and Kuriyan, J (1997) Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III. Cell 91:335-45
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.
Links	PubMed
Keywords	Adenosine Triphosphate/metabolism; Amino Acid Sequence; Crystallography, X-Ray; DNA Polymerase III/chemistry; DNA Polymerase III/metabolism; Escherichia coli/enzymology; Hydrolysis; Models, Molecular; Molecular Sequence Data; Phosphates/metabolism; Protein Conformation; Sequence Homology, Amino Acid
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