7V3U
Cryo-EM structure of MCM double hexamer with structured Mcm4-NSD
This is a non-PDB format compatible entry.
Summary for 7V3U
| Entry DOI | 10.2210/pdb7v3u/pdb |
| EMDB information | 31684 |
| Descriptor | DNA replication licensing factor MCM2, ADENOSINE-5'-DIPHOSPHATE, DNA replication licensing factor MCM3, ... (10 entities in total) |
| Functional Keywords | dna replication initiation, complex, replicative helicase, replication, cell cycle |
| Biological source | Saccharomyces cerevisiae S288C More |
| Total number of polymer chains | 12 |
| Total formula weight | 1219771.11 |
| Authors | |
| Primary citation | Cheng, J.,Li, N.,Huo, Y.,Dang, S.,Tye, B.K.,Gao, N.,Zhai, Y. Structural Insight into the MCM double hexamer activation by Dbf4-Cdc7 kinase. Nat Commun, 13:1396-1396, 2022 Cited by PubMed Abstract: The Dbf4-dependent kinase Cdc7 (DDK) regulates DNA replication initiation by phosphorylation of the MCM double hexamer (MCM-DH) to promote helicase activation. Here, we determine a series of cryo electron microscopy (cryo-EM) structures of yeast DDK bound to the MCM-DH. These structures, occupied by one or two DDKs, differ primarily in the conformations of the kinase core. The interactions of DDK with the MCM-DH are mediated exclusively by subunit Dbf4 straddling across the hexamer interface on the three N-terminal domains (NTDs) of subunits Mcm2, Mcm6, and Mcm4. This arrangement brings Cdc7 close to its only essential substrate, the N-terminal serine/threonine-rich domain (NSD) of Mcm4. Dbf4 further displaces the NSD from its binding site on Mcm4-NTD, facilitating an immediate targeting of this motif by Cdc7. Moreover, the active center of Cdc7 is occupied by a unique Dbf4 inhibitory loop, which is disengaged when the kinase core assumes wobbling conformations. This study elucidates the versatility of Dbf4 in regulating the ordered multisite phosphorylation of the MCM-DH by Cdc7 kinase during helicase activation. PubMed: 35296675DOI: 10.1038/s41467-022-29070-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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