Fig. 3: ATP and DNA binding in the dCMGE complex.
From: Mechanism of replication origin melting nucleated by CMG helicase assembly
a, MCM nucleotide occupancy in the double hexamer and in the dCMGE complex. b, Surface rendering of the nucleotide in the six ATPase sites of MCM. c, Duplex DNA binding in the dCMGE complex (left) explains how the double-hexamer-to-dCMGE transition leads to selection of the translocation strand. The ATPase pore loops in the dCMGE complex only contact the leading-strand template. The density for the selected translocation strand (red on the right) has been extracted from the duplex DNA density (grey on the left). d, The leading-strand template extracted from the dCMGE structure superposed on the yeast CMG translocating on a DNA fork reconstituted on an artificial DNA fork (PDB 6U0M), bound to the fork stabilization complex (PDB 6SKL) or bound to SCFDia2 and duplex DNA (PDB 7PMK).
