Cell. 1997 Oct 31;91(3):335-45.

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.

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The Rockefeller University, New York, New York 10021, USA.

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.

PMID:: 9363942; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Crystal Structure Of The Delta Prime Subunit Of The Clamp- Loader Complex Of Escherichia Coli Dna Polymerase Iii

PDB: 1A5T

Source: Escherichia coli

Method: X-Ray Diffraction

Resolution: 2.2 Å

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