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8P5E

S. cerevisiae nexus-sCMGE after DNA replication initiation

This is a non-PDB format compatible entry.
Summary for 8P5E
Entry DOI10.2210/pdb8p5e/pdb
EMDB information17449
DescriptorDNA replication licensing factor MCM2, DNA replication complex GINS protein SLD5, Cell division control protein 45, ... (19 entities in total)
Functional Keywordssaccharomyces cerevisiae, helicase, cmge, initiation of dna replication, dna, dna unwinding, replication
Biological sourceSaccharomyces cerevisiae (brewer's yeast)
More
Total number of polymer chains15
Total formula weight1140442.35
Authors
Henrikus, S.S.,Willhoft, O. (deposition date: 2023-05-24, release date: 2024-05-29, Last modification date: 2024-08-28)
Primary citationHenrikus, S.S.,Gross, M.H.,Willhoft, O.,Puhringer, T.,Lewis, J.S.,McClure, A.W.,Greiwe, J.F.,Palm, G.,Nans, A.,Diffley, J.F.X.,Costa, A.
Unwinding of a eukaryotic origin of replication visualized by cryo-EM.
Nat.Struct.Mol.Biol., 31:1265-1276, 2024
Cited by
PubMed Abstract: To prevent detrimental chromosome re-replication, DNA loading of a double hexamer of the minichromosome maintenance (MCM) replicative helicase is temporally separated from DNA unwinding. Upon S-phase transition in yeast, DNA unwinding is achieved in two steps: limited opening of the double helix and topological separation of the two DNA strands. First, Cdc45, GINS and Polε engage MCM to assemble a double CMGE with two partially separated hexamers that nucleate DNA melting. In the second step, triggered by Mcm10, two CMGEs separate completely, eject the lagging-strand template and cross paths. To understand Mcm10 during helicase activation, we used biochemical reconstitution with cryogenic electron microscopy. We found that Mcm10 splits the double CMGE by engaging the N-terminal homo-dimerization face of MCM. To eject the lagging strand, DNA unwinding is started from the N-terminal side of MCM while the hexamer channel becomes too narrow to harbor duplex DNA.
PubMed: 38760633
DOI: 10.1038/s41594-024-01280-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

227561

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