PMID:11525729
| Citation |
Jeruzalmi, D, O'Donnell, M and Kuriyan, J (2001) Crystal structure of the processivity clamp loader gamma (gamma) complex of E. coli DNA polymerase III. Cell 106:429-41 |
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| Abstract |
The gamma complex, an AAA+ ATPase, is the bacterial homolog of eukaryotic replication factor C (RFC) that loads the sliding clamp (beta, homologous to PCNA) onto DNA. The 2.7/3.0 A crystal structure of gamma complex reveals a pentameric arrangement of subunits, with stoichiometry delta':gamma(3):delta. The C-terminal domains of the subunits form a circular collar that supports an asymmetric arrangement of the N-terminal ATP binding domains of the gamma motor and the structurally related domains of the delta' stator and the delta wrench. The structure suggests a mechanism by which the gamma complex switches between a closed state, in which the beta-interacting element of delta is hidden by delta', and an open form similar to the crystal structure, in which delta is free to bind to beta. |
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| Keywords |
Binding Sites; Crystallography, X-Ray; DNA-Directed DNA Polymerase/chemistry; DNA-Directed DNA Polymerase/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Macromolecular Substances; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Quaternary; Protein Structure, Tertiary |
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This is the first X-stal structure of the DNA polymerase III clamp loader.
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