8FOD
Cryo-EM structure of S. cerevisiae DNA polymerase alpha-primase complex in Apo state conformation II
Summary for 8FOD
| Entry DOI | 10.2210/pdb8fod/pdb |
| EMDB information | 29346 |
| Descriptor | DNA polymerase, DNA primase, DNA primase large subunit, ... (5 entities in total) |
| Functional Keywords | dna polymerase, primase, dna replication, dna binding protein |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 4 |
| Total formula weight | 356354.26 |
| Authors | Yuan, Z.,Georgescu, R.,Li, H.,O'Donnell, M. (deposition date: 2022-12-30, release date: 2023-05-31, Last modification date: 2024-03-13) |
| Primary citation | Yuan, Z.,Georgescu, R.,Li, H.,O'Donnell, M.E. Molecular choreography of primer synthesis by the eukaryotic Pol alpha-primase. Nat Commun, 14:3697-3697, 2023 Cited by PubMed Abstract: The eukaryotic polymerase α (Pol α) synthesizes an RNA-DNA hybrid primer of 20-30 nucleotides. Pol α is composed of Pol1, Pol12, Primase 1 (Pri1), and Pri2. Pol1 and Pri1 contain the DNA polymerase and RNA primase activities, respectively. It has been unclear how Pol α hands over an RNA primer from Pri1 to Pol1 for DNA primer extension, and how the primer length is defined. Here we report the cryo-EM analysis of yeast Pol α in the apo, primer initiation, primer elongation, RNA primer hand-off from Pri1 to Pol1, and DNA extension states, revealing a series of very large movements. We reveal a critical point at which Pol1-core moves to take over the 3'-end of the RNA from Pri1. DNA extension is limited by a spiral motion of Pol1-core. Since both Pri1 and Pol1-core are flexibly attached to a stable platform, primer growth produces stress that limits the primer length. PubMed: 37344454DOI: 10.1038/s41467-023-39441-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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