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5XF8

Cryo-EM structure of the Cdt1-MCM2-7 complex in AMPPNP state

Replaces:  5H7I
Summary for 5XF8
Entry DOI10.2210/pdb5xf8/pdb
EMDB information6671
DescriptorDNA replication licensing factor MCM2, DNA replication licensing factor MCM3, DNA replication licensing factor MCM4, ... (7 entities in total)
Functional Keywordshelicase, dna replication, hydrolase
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Cellular locationNucleus: P29469 P24279 P30665 P29496 P53091
Cytoplasm : P38132 P47112
Total number of polymer chains7
Total formula weight677976.49
Authors
Zhai, Y.,Cheng, E.,Wu, H.,Li, N.,Yung, P.Y.,Gao, N.,Tye, B.K. (deposition date: 2017-04-09, release date: 2017-05-03)
Primary citationZhai, Y.,Cheng, E.,Wu, H.,Li, N.,Yung, P.Y.,Gao, N.,Tye, B.K.
Open-ringed structure of the Cdt1-Mcm2-7 complex as a precursor of the MCM double hexamer
Nat. Struct. Mol. Biol., 24:300-308, 2017
Cited by
PubMed Abstract: 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-Å 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.
PubMed: 28191894
DOI: 10.1038/nsmb.3374
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.1 Å)
Structure validation

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