1NJG

Nucleotide-free form of an Isolated E. coli Clamp Loader Gamma Subunit

Summary for 1NJG

• Entry DOI: 10.2210/pdb1njg/pdb
• Related: 1NJF
• Descriptor: DNA polymerase III subunit gamma, ZINC ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: rossman-like fold, aaa+ atpase domains, sensor 1, sensor 2, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 55417.87

Authors

Podobnik, M.,Weitze, T.F.,O'Donnell, M.,Kuriyan, J. (deposition date: 2002-12-30, release date: 2003-04-01, Last modification date: 2023-08-16)

Primary citation

Podobnik, M.,Weitze, T.F.,O'Donnell, M.,Kuriyan, J.
Nucleotide-Induced Conformational Changes in an Isolated Escherichia coli DNA Polymerase III Clamp Loader Subunit
Structure, 11:253-263, 2003

PubMed 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.

PubMed: 12623013
DOI: 10.1016/S0969-2126(03)00027-3

Experimental method

X-RAY DIFFRACTION (2.2 Å)