Crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III.
Cell
; 91(3): 335-45, 1997 Oct 31.
Article
de En
| MEDLINE
| ID: mdl-9363942
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.
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Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
DNA polymerase III
/
Escherichia coli
Langue:
En
Journal:
Cell
Année:
1997
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique