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.

Polymerases:

Topics:

Structure and Structure/Function

Status:

new topics/pols set partial results complete validated

Results:

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Entry validated by:

Structures:

1A5T
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