1a5t

Publication Abstract from PubMed

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.

Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III.,Guenther B, Onrust R, Sali A, O'Donnell M, Kuriyan J Cell. 1997 Oct 31;91(3):335-45. PMID:9363942^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.