8v6j | pdb_00008v6j

DNA elongation complex (configuration 2) of Xenopus laevis DNA polymerase alpha-primase

spinqualitylabelsall models 8v6j, resolution 11.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8v6j is a 6 chain structure with sequence from Xenopus laevis and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 11.11Å Ligands: DGT, DOC, GTP, MG, SF4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q800A4_XENLA Publication Abstract from PubMed The mechanism by which polymerase alpha-primase (polalpha-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 polalpha-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 polalpha and increases polalpha 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 polalpha 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 polalpha-primase. A mechanistic model of primer synthesis from catalytic structures of DNA polymerase alpha-primase.,Mullins EA, Salay LE, Durie CL, Bradley NP, Jackman JE, Ohi MD, Chazin WJ, Eichman BF Nat Struct Mol Biol. 2024 May;31(5):777-790. doi: 10.1038/s41594-024-01227-4. , Epub 2024 Mar 15. PMID:38491139 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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