2IDO
Structure of the E. coli Pol III epsilon-Hot proofreading complex
Summary for 2IDO
| Entry DOI | 10.2210/pdb2ido/pdb |
| Descriptor | DNA polymerase III epsilon subunit, Hot protein, MANGANESE (II) ION, ... (6 entities in total) |
| Functional Keywords | polymerase, exonuclease, hot, epsilon, pol iii, transferase |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 61884.49 |
| Authors | Kirby, T.W.,Harvey, S.,DeRose, E.F.,Chalov, S.,Chikova, A.K.,Perrino, F.W.,Schaaper, R.M.,London, R.E.,Pedersen, L.C. (deposition date: 2006-09-15, release date: 2006-11-14, Last modification date: 2023-08-30) |
| Primary citation | Kirby, T.W.,Harvey, S.,DeRose, E.F.,Chalov, S.,Chikova, A.K.,Perrino, F.W.,Schaaper, R.M.,London, R.E.,Pedersen, L.C. Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex. J.Biol.Chem., 281:38466-38471, 2006 Cited by PubMed Abstract: The epsilon subunit of Escherichia coli DNA polymerase III possesses 3'-exonucleolytic proofreading activity. Within the Pol III core, epsilon is tightly bound between the alpha subunit (DNA polymerase) and subunit. Here, we present the crystal structure of epsilon in complex with HOT, the bacteriophage P1-encoded homolog of , at 2.1 A resolution. The epsilon-HOT interface is defined by two areas of contact: an interaction of the previously unstructured N terminus of HOT with an edge of the epsilon central beta-sheet as well as interactions between HOT and the catalytically important helix alpha1-loop-helix alpha2 motif of epsilon. This structure provides insight into how HOT and, by implication, may stabilize the epsilon subunit, thus promoting efficient proofreading during chromosomal replication. PubMed: 16973612DOI: 10.1074/jbc.M606917200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
Download full validation report
