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Structure paper

TitleStructures of human primosome elongation complexes.
Journal, issue, pagesNat Struct Mol Biol, Vol. 30, Issue 5, Page 579-583, Year 2023
Publish dateApr 17, 2023
AuthorsQixiang He / Andrey G Baranovskiy / Lucia M Morstadt / Alisa E Lisova / Nigar D Babayeva / Benjamin L Lusk / Ci Ji Lim / Tahir H Tahirov /
PubMed AbstractThe 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. ...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.
External linksNat Struct Mol Biol / PubMed:37069376 / PubMed Central
MethodsEM (single particle)
Resolution3.35 - 3.59 Å
Structure data

27256

8d96

EMDB-27256, PDB-8d96:
Human DNA polymerase alpha/primase elongation complex I bound to primer/template
Method: EM (single particle) / Resolution: 3.35 Å

27258

8d9d

EMDB-27258, PDB-8d9d:
Human DNA polymerase-alpha/primase elongation complex II bound to primer/template
Method: EM (single particle) / Resolution: 3.59 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-MG:
Unknown entry

ChemComp-DTP:
2'-DEOXYADENOSINE 5'-TRIPHOSPHATE

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsREPLICATION / DNA replication / human DNA polymerase alpha/primase / human primosome / elongation complex

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