期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 20, 期 8, 页码 944-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2629
关键词
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资金
- US National Institutes of Health [GM45436, GM74985]
- United Kingdom Medical Research Council
- Japan Society for the Promotion of Science
- Uehara Memorial Foundation
- MRC [MC_U120085811] Funding Source: UKRI
- Medical Research Council [MC_U120085811] Funding Source: researchfish
- Grants-in-Aid for Scientific Research [24870021] Funding Source: KAKEN
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-gamma S, 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.
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