Structural Insight into the MCM double hexamer activation by Dbf4-Cdc7 kinase
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 …
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 …
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