9C51
Cryo-EM structure of the Strand displacement Complex (IV) of Yeast Mitochondrial DNA polymerase Gamma (MIP1) with downstream DNA
Summary for 9C51
| Entry DOI | 10.2210/pdb9c51/pdb |
| EMDB information | 45194 |
| Descriptor | DNA polymerase gamma, Non-Template DNA, Primer DNA, ... (6 entities in total) |
| Functional Keywords | mitochondrial dna polymerase gamma, strand displacement complex, mip1, replication, helicase independent dna polymerase, transferase-dna complex, transferase/dna |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) More |
| Total number of polymer chains | 4 |
| Total formula weight | 169654.50 |
| Authors | Nayak, A.R.,Sokolova, V.O.,Sillamaa, S.,Sedmen, J.,Temiakov, D. (deposition date: 2024-06-05, release date: 2025-03-19, Last modification date: 2025-03-26) |
| Primary citation | Nayak, A.R.,Sokolova, V.,Sillamaa, S.,Herbine, K.,Sedman, J.,Temiakov, D. Structural basis for intrinsic strand displacement activity of mitochondrial DNA polymerase. Nat Commun, 16:2417-2417, 2025 Cited by PubMed Abstract: Members of the Pol A family of DNA polymerases, found across all domains of life, utilize various strategies for DNA strand separation during replication. In higher eukaryotes, mitochondrial DNA polymerase γ relies on the replicative helicase TWINKLE, whereas the yeast ortholog, Mip1, can unwind DNA independently. Using Mip1 as a model, we present a series of high-resolution cryo-EM structures that capture the process of DNA strand displacement. Our data reveal previously unidentified structural elements that facilitate the unwinding of the downstream DNA duplex. Yeast cells harboring Mip1 variants defective in strand displacement exhibit impaired oxidative phosphorylation and loss of mtDNA, corroborating the structural observations. This study provides a molecular basis for the intrinsic strand displacement activity of Mip1 and illuminates the distinct unwinding mechanisms utilized by Pol A family DNA polymerases. PubMed: 40069189DOI: 10.1038/s41467-025-57594-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.42 Å) |
Structure validation
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