Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 24, Issue 3, Pages 300-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3374
Keywords
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Funding
- Ministry of Science and Technology of China [2013CB910404, 2016YFA0500700]
- National Natural Science Foundation of China [31422016, 31470722, 31630087]
- Research Grants Council of Hong Kong [GRF16138716, GRF664013, HKUST12/CRF/13G, GRF16104115, GRF16143016, IGN15SC02]
- Peking-Tsinghua Center for Life Sciences
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The minichromosome maintenance complex (MCM) hexameric complex (Mcm2-7) forms the core of the eukaryotic replicative helicase. During G1 phase, two Cdt1-Mcm2-7 heptamers are loaded onto each replication origin by the origin-recognition complex (ORC) and Cdc6 to form an inactive MCM double hexamer (DH), but the detailed loading mechanism remains unclear. Here we examine the structures of the yeast MCM hexamer and Cdt1-MCM heptamer from Saccharomyces cerevisiae. Both complexes form left-handed coil structures with a 10-15-angstrom gap between Mcm5 and Mcm2, and a central channel that is occluded by the C-terminal domain winged-helix motif of Mcm5. Cdt1 wraps around the N-terminal regions of Mcm2, Mcm6 and Mcm4 to stabilize the whole complex. The intrinsic coiled structures of the precursors provide insights into the DH formation, and suggest a spring-action model for the MCM during the initial origin melting and the subsequent DNA unwinding.
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