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TitleCryo-EM structure of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 bound to DNA.
Journal, issue, pagesNat Struct Mol Biol, Vol. 20, Issue 8, Page 944-951, Year 2013
Publish dateJul 14, 2013
AuthorsJingchuan Sun / Cecile Evrin / Stefan A Samel / Alejandra Fernández-Cid / Alberto Riera / Hironori Kawakami / Bruce Stillman / Christian Speck / Huilin Li /
PubMed AbstractIn eukaryotes, the Cdt1-bound replicative helicase core MCM2-7 is loaded onto DNA by the ORC-Cdc6 ATPase to form a prereplicative complex (pre-RC) with an MCM2-7 double hexamer encircling DNA. Using ...In eukaryotes, the Cdt1-bound replicative helicase core MCM2-7 is loaded onto DNA by the ORC-Cdc6 ATPase to form a prereplicative complex (pre-RC) with an MCM2-7 double hexamer encircling DNA. Using purified components in the presence of ATP-γS, we have captured in vitro an intermediate in pre-RC assembly that contains a complex between the ORC-Cdc6 and Cdt1-MCM2-7 heteroheptamers called the OCCM. Cryo-EM studies of this 14-subunit complex reveal that the two separate heptameric complexes are engaged extensively, with the ORC-Cdc6 N-terminal AAA+ domains latching onto the C-terminal AAA+ motor domains of the MCM2-7 hexamer. The conformation of ORC-Cdc6 undergoes a concerted change into a right-handed spiral with helical symmetry that is identical to that of the DNA double helix. The resulting ORC-Cdc6 helicase loader shows a notable structural similarity to the replication factor C clamp loader, suggesting a conserved mechanism of action.
External linksNat Struct Mol Biol / PubMed:23851460 / PubMed Central
MethodsEM (single particle)
Resolution14.0 Å
Structure data

EMDB-5625:
Architecture of a helicase loading intermediate containing ORC-Cdc6-Cdt1-MCM2-7 on DNA reveals similarity to DNA polymerase clamp loading complexes
Method: EM (single particle) / Resolution: 14.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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