Summary for 5XF8
| Entry DOI | 10.2210/pdb5xf8/pdb |
| EMDB information | 6671 |
| Descriptor | DNA replication licensing factor MCM2, DNA replication licensing factor MCM3, DNA replication licensing factor MCM4, ... (7 entities in total) |
| Functional Keywords | helicase, dna replication, hydrolase |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Cellular location | Nucleus: P29469 P24279 P30665 P29496 P53091 Cytoplasm : P38132 P47112 |
| Total number of polymer chains | 7 |
| Total formula weight | 677976.49 |
| Authors | |
| Primary citation | Zhai, 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: 28191894DOI: 10.1038/nsmb.3374 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.1 Å) |
Structure validation
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