1NJF
Nucleotide bound form of an isolated E. coli clamp loader gamma subunit
Summary for 1NJF
| Entry DOI | 10.2210/pdb1njf/pdb |
| Related | 1NJG |
| Descriptor | DNA polymerase III subunit gamma, ZINC ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (5 entities in total) |
| Functional Keywords | protein-nucleotide complex, rossman-like fold, aaa+ atpase domains, sensor 1, sensor 2, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 112256.30 |
| Authors | Podobnik, M.,Weitze, T.F.,O'Donnell, M.,Kuriyan, J. (deposition date: 2002-12-30, release date: 2003-04-08, Last modification date: 2024-02-14) |
| 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 Cited by 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: 12623013DOI: 10.1016/S0969-2126(03)00027-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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