Cryo-EM structure of a helicase loading intermediate containing ORC–Cdc6–Cdt1–MCM2-7 bound to DNA View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-08

AUTHORS

Jingchuan Sun, Cecile Evrin, Stefan A Samel, Alejandra Fernández-Cid, Alberto Riera, Hironori Kawakami, Bruce Stillman, Christian Speck, Huilin Li

ABSTRACT

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. More... »

PAGES

944-951

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb.2629

DOI

http://dx.doi.org/10.1038/nsmb.2629

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017369330

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23851460


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