Fig. 2
From: Cryo-EM structure of a licensed DNA replication origin
Near atomic resolution model of MCM and nucleotide occupancy of the ATPase motor. a 4.3 Å resolution structure of the phosphorylated MCM and a detail of the dimerization interface shown on the right. b On the left: atomic model of the MCM ATPase motor, overlaid with the nucleotide density recovered in between AAA+ protomers. Mcm5-3 and Mcm5-2 contain strong nucleotide density peaks. The same ATPase site profile can be observed for the unphosphorylated form of MCM. Mcm2-6 is nucleotide free and in a relaxed configuration favouring ADP release. On the right: atomic model of ATP-CMG. Mcm5-3, Mcm2-5 and Mcm6-2 are bound to ATP
