4M8O
TERNARY COMPLEX OF DNA POLYMERASE EPSILON WITH AN INCOMING dATP
Summary for 4M8O
| Entry DOI | 10.2210/pdb4m8o/pdb |
| Descriptor | DNA polymerase epsilon catalytic subunit A, PRIMER DNA, TEMPLATE DNA, ... (9 entities in total) |
| Functional Keywords | dna polymerase b type, dna synthesis, protein-dna complex, dna replication, metal-binding, transferase dna complex, nucleotidyltransferase, transferase-dna complex, transferase/dna |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Cellular location | Nucleus: P21951 |
| Total number of polymer chains | 3 |
| Total formula weight | 152226.41 |
| Authors | Sauer-Eriksson, A.E.,Hogg, M.,Osterman, P.,Johansson, E. (deposition date: 2013-08-13, release date: 2013-11-27, Last modification date: 2023-09-20) |
| Primary citation | Hogg, M.,Osterman, P.,Bylund, G.O.,Ganai, R.A.,Lundstrom, E.B.,Sauer-Eriksson, A.E.,Johansson, E. Structural basis for processive DNA synthesis by yeast DNA polymerase epsilon. Nat.Struct.Mol.Biol., 21:49-55, 2014 Cited by PubMed Abstract: DNA polymerase ɛ (Pol ɛ) is a high-fidelity polymerase that has been shown to participate in leading-strand synthesis during DNA replication in eukaryotic cells. We present here a ternary structure of the catalytic core of Pol ɛ (142 kDa) from Saccharomyces cerevisiae in complex with DNA and an incoming nucleotide. This structure provides information about the selection of the correct nucleotide and the positions of amino acids that might be critical for proofreading activity. Pol ɛ has the highest fidelity among B-family polymerases despite the absence of an extended β-hairpin loop that is required for high-fidelity replication by other B-family polymerases. Moreover, the catalytic core has a new domain that allows Pol ɛ to encircle the nascent double-stranded DNA. Altogether, the structure provides an explanation for the high processivity and high fidelity of leading-strand DNA synthesis in eukaryotes. PubMed: 24292646DOI: 10.1038/nsmb.2712 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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