1J53
Structure of the N-terminal Exonuclease Domain of the Epsilon Subunit of E.coli DNA Polymerase III at pH 8.5
Summary for 1J53
| Entry DOI | 10.2210/pdb1j53/pdb |
| Related | 1J54 |
| Descriptor | DNA polymerase III, epsilon chain, MANGANESE (II) ION, THYMIDINE-5'-PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | dna polymerase proofreading domain, transferase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 21620.12 |
| Authors | Hamdan, S.,Carr, P.D.,Brown, S.E.,Ollis, D.L.,Dixon, N.E. (deposition date: 2002-01-22, release date: 2002-10-16, Last modification date: 2024-12-25) |
| Primary citation | Hamdan, S.,Carr, P.D.,Brown, S.E.,Ollis, D.L.,Dixon, N.E. Structural Basis for Proofreading during Replication of the Escherichia coli Chromosome Structure, 10:535-546, 2002 Cited by PubMed Abstract: The epsilon subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3'-5' exonuclease. Structures of its catalytic N-terminal domain (epsilon186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 A, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5'-monophosphate. The protein structure is built around a core five-stranded beta sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for epsilon and to produce a plausible model of the complex of epsilon186 with DNA. PubMed: 11937058DOI: 10.1016/S0969-2126(02)00738-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
