2HPM
Eubacterial and Eukaryotic Replicative DNA Polymerases are not Homologous: X-ray Structure of DNA Polymerase III
Summary for 2HPM
Entry DOI | 10.2210/pdb2hpm/pdb |
Related | 2HPI |
Descriptor | DNA Polymerase III alpha subunit, ZINC ION, MAGNESIUM ION, ... (5 entities in total) |
Functional Keywords | nucleotidyltransferase fold, transferase |
Biological source | Thermus aquaticus |
Cellular location | Cytoplasm (By similarity): Q9XDH5 |
Total number of polymer chains | 1 |
Total formula weight | 138087.71 |
Authors | Bailey, S.,Wing, R.A.,Steitz, T.A. (deposition date: 2006-07-17, release date: 2006-09-19, Last modification date: 2024-02-14) |
Primary citation | Bailey, S.,Wing, R.A.,Steitz, T.A. The Structure of T. aquaticus DNA Polymerase III Is Distinct from Eukaryotic Replicative DNA Polymerases. Cell(Cambridge,Mass.), 126:893-904, 2006 Cited by PubMed Abstract: The crystal structure of Thermus aquaticus DNA polymerase III alpha subunit reveals that the structure of the catalytic domain of the eubacterial replicative polymerase is unrelated to that of the eukaryotic replicative polymerase but rather belongs to the Polbeta-like nucleotidyltransferase superfamily. A model of the polymerase complexed with both DNA and beta-sliding clamp interacting with a reoriented binding domain and internal beta binding site was constructed that is consistent with existing biochemical data. Within the crystal, two C-terminal domains are interacting through a surface that is larger than many dimer interfaces. Since replicative polymerases of eubacteria and eukaryotes/archaea are not homologous, the nature of the replicative polymerase in the last common ancestor is unknown. Although other possibilities have been proposed, the plausibility of a ribozyme DNA polymerase should be considered. PubMed: 16959569DOI: 10.1016/j.cell.2006.07.027 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.7 Å) |
Structure validation
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