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8G9F

Complete auto-inhibitory complex of Xenopus laevis DNA polymerase alpha-primase

Summary for 8G9F
Entry DOI10.2210/pdb8g9f/pdb
EMDB information29862 29864 29871 29872 29873 29886 29888 29889 29891
DescriptorDNA polymerase alpha catalytic subunit, DNA polymerase alpha subunit B, DNA primase large subunit, ... (6 entities in total)
Functional Keywordsprimase, dna polymerase, chimeric rna-dna primer, rna/dna hybrid, dna replication, dna synthesis, replication, transferase
Biological sourceXenopus laevis (African clawed frog)
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Total number of polymer chains4
Total formula weight305781.73
Authors
Mullins, E.A.,Chazin, W.J.,Eichman, B.F. (deposition date: 2023-02-21, release date: 2023-04-12, Last modification date: 2024-05-29)
Primary citationMullins, E.A.,Salay, L.E.,Durie, C.L.,Bradley, N.P.,Jackman, J.E.,Ohi, M.D.,Chazin, W.J.,Eichman, B.F.
A mechanistic model of primer synthesis from catalytic structures of DNA polymerase alpha-primase.
Nat.Struct.Mol.Biol., 31:777-790, 2024
Cited by
PubMed Abstract: The mechanism by which polymerase α-primase (polα-primase) synthesizes chimeric RNA-DNA primers of defined length and composition, necessary for replication fidelity and genome stability, is unknown. Here, we report cryo-EM structures of Xenopus laevis polα-primase in complex with primed templates representing various stages of DNA synthesis. Our data show how interaction of the primase regulatory subunit with the primer 5' end facilitates handoff of the primer to polα and increases polα processivity, thereby regulating both RNA and DNA composition. The structures detail how flexibility within the heterotetramer enables synthesis across two active sites and provide evidence that termination of DNA synthesis is facilitated by reduction of polα and primase affinities for the varied conformations along the chimeric primer-template duplex. Together, these findings elucidate a critical catalytic step in replication initiation and provide a comprehensive model for primer synthesis by polα-primase.
PubMed: 38491139
DOI: 10.1038/s41594-024-01227-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

226707

건을2024-10-30부터공개중

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