1a5t

From Proteopedia

Revision as of 12:32, 5 November 2007

CRYSTAL STRUCTURE OF THE DELTA PRIME SUBUNIT OF THE CLAMP-LOADER COMPLEX OF ESCHERICHIA COLI DNA POLYMERASE III

Overview

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.

About this Structure

1A5T is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Structure known Active Site: ZNB. Full crystallographic information is available from OCA.

Reference

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

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