1A5T

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

Summary for 1A5T

• Entry DOI: 10.2210/pdb1a5t/pdb
• Descriptor: DELTA PRIME, ZINC ION (3 entities in total)
• Functional Keywords: zinc finger, dna replication
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 37045.89

Authors

Guenther, B.,Onrust, R.,Sali, A.,O'Donnell, M.,Kuriyan, J. (deposition date: 1998-02-18, release date: 1998-05-27, Last modification date: 2024-02-07)

Primary citation

Guenther, B.,Onrust, R.,Sali, A.,O'Donnell, M.,Kuriyan, J.
Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III.
Cell(Cambridge,Mass.), 91:335-345, 1997

PubMed 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.

PubMed: 9363942
DOI: 10.1016/S0092-8674(00)80417-1

Experimental method

X-RAY DIFFRACTION (2.2 Å)