8D96

Human DNA polymerase alpha/primase elongation complex I bound to primer/template

Summary for 8D96

• Entry DOI: 10.2210/pdb8d96/pdb
• Related: 8D9D
• EMDB information: 27256 27258
• Descriptor: DNA primase large subunit, DNA polymerase alpha catalytic subunit, DNA/RNA (5'-GTP)-R(P*GP*CP*GP*GP*CP*AP*CP*G)-D(P*AP*CP*C)-3'), ... (7 entities in total)
• Functional Keywords: dna replication, human dna polymerase alpha/primase, human primosome, elongation complex, replication
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 4
• Total formula weight: 236626.88

Authors

He, Q.,Baranovskiy, A.,Lim, C.,Tahirov, T. (deposition date: 2022-06-09, release date: 2023-04-19, Last modification date: 2024-06-12)

Primary citation

He, Q.,Baranovskiy, A.G.,Morstadt, L.M.,Lisova, A.E.,Babayeva, N.D.,Lusk, B.L.,Lim, C.J.,Tahirov, T.H.
Structures of human primosome elongation complexes.
Nat.Struct.Mol.Biol., 30:579-583, 2023

PubMed Abstract: The synthesis of RNA-DNA primer by primosome requires coordination between primase and DNA polymerase α subunits, which is accompanied by unknown architectural rearrangements of multiple domains. Using cryogenic electron microscopy, we solved a 3.6 Å human primosome structure caught at an early stage of RNA primer elongation with deoxynucleotides. The structure confirms a long-standing role of primase large subunit and reveals new insights into how primosome is limited to synthesizing short RNA-DNA primers.

PubMed: 37069376
DOI: 10.1038/s41594-023-00971-3

Experimental method

ELECTRON MICROSCOPY (3.35 Å)