Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	A mechanistic model of primer synthesis from catalytic structures of DNA polymerase α-primase.
Journal, issue, pages	Nat Struct Mol Biol, Vol. 31, Issue 5, Page 777-790, Year 2024
Publish date	Mar 15, 2024
Authors	Elwood A Mullins / Lauren E Salay / Clarissa L Durie / Noah P Bradley / Jane E Jackman / Melanie D Ohi / Walter J Chazin / Brandt F Eichman /
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 ...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.
External links	Nat Struct Mol Biol / PubMed:38491139 / PubMed Central
Methods	EM (single particle)
Resolution	2.8 - 14.06 Å
Structure data	29862 8g99 EMDB-29862, PDB-8g99: Partial auto-inhibitory complex of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 2.8 Å 29864 8g9f EMDB-29864, PDB-8g9f: Complete auto-inhibitory complex of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 3.2 Å 29871 8g9l EMDB-29871, PDB-8g9l: DNA initiation subcomplex of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 3.3 Å 29872 8g9n EMDB-29872, PDB-8g9n: Partial DNA elongation subcomplex of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 3.5 Å 29873 8g9o EMDB-29873, PDB-8g9o: Complete DNA elongation subcomplex of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 4.4 Å 29888 8v5m EMDB-29888, PDB-8v5m: Tetramer core subcomplex (conformation 1) of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 5.3 Å 29889 8v5n EMDB-29889, PDB-8v5n: Tetramer core subcomplex (conformation 2) of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 4.2 Å 29891 8v5o EMDB-29891, PDB-8v5o: Tetramer core subcomplex (conformation 3) of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 4.7 Å 42140 8ucu EMDB-42140, PDB-8ucu: Partial DNA termination subcomplex of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 2.85 Å 42141 8ucv EMDB-42141, PDB-8ucv: Complete DNA termination subcomplex 1 of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 3.81 Å 42142 8ucw EMDB-42142, PDB-8ucw: Complete DNA termination subcomplex 2 of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 3.64 Å 42990 8v6g EMDB-42990, PDB-8v6g: DNA initiation complex (configuration 1) of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 11.16 Å 42991 8v6h EMDB-42991, PDB-8v6h: DNA initiation complex (configuration 2) of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 11.11 Å 42992 8v6i EMDB-42992, PDB-8v6i: DNA elongation complex (configuration 1) of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 14.06 Å 42993 8v6j EMDB-42993, PDB-8v6j: DNA elongation complex (configuration 2) of Xenopus laevis DNA polymerase alpha-primase Method: EM (single particle) / Resolution: 11.11 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-SF4: IRON/SULFUR CLUSTER ChemComp-DGT: 2'-DEOXYGUANOSINE-5'-TRIPHOSPHATE ChemComp-MG: Unknown entry
Source	xenopus laevis (African clawed frog) synthetic construct (others)
Keywords	REPLICATION / TRANSFERASE / Primase / DNA polymerase / chimeric RNA-DNA primer / RNA/DNA hybrid / DNA replication / DNA synthesis / TRANSFERASE/DNA/RNA / TRANSFERASE-DNA-RNA complex