PMID:12623013

Citation	Podobnik, M, Weitze, TF, O'Donnell, M and Kuriyan, J (2003) Nucleotide-induced conformational changes in an isolated Escherichia coli DNA polymerase III clamp loader subunit. Structure 11:253-63
Abstract	Sliding clamps are loaded onto DNA by ATP-driven clamp loader complexes. The structure of the E. coli clamp loader in a nucleotide-free state has been determined previously. We now report crystal structures of a truncated form of the isolated gamma-ATPase subunit, gamma(1-243), of the E. coli clamp loader, in nucleotide-free and bound forms. The gamma subunit adopts a defined conformation when empty, in which the nucleotide binding site is blocked. The binding of either ATPgammaS or ADP, which are shown to bind with equal affinity to gamma(1-243), induces a change in the relative orientation of the two domains such that nucleotides can be accommodated. This change would break one of the gamma:gamma interfaces seen in the empty clamp loader complex, and may represent one step in the activation process.
Links	PubMed
Keywords	Adenosine Triphosphatases/metabolism; DNA/metabolism; DNA Polymerase III/metabolism; Escherichia coli/enzymology; Protein Conformation; Protein Structure, Quaternary; Pyrococcus furiosus/enzymology
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