Fig. 5 | Nature Communications

Fig. 5

From: Structure of DNA-CMG-Pol epsilon elucidates the roles of the non-catalytic polymerase modules in the eukaryotic replisome

Fig. 5

ATPase state and DNA binding in the CMG-Pol epsilon complex. a Inspection of the local resolution map indicates that the ATPase site clamped by C-Pol2/Dpb2 is highly stable, with the Mcm5 AAA+ module reaching resolutions as high as 4.5 Å. b Single-stranded DNA is captured by ATPase pore loops of Mcm3, -5, -2, and -6. ATPγS is bound to the Mcm5-3 and Mcm2-5 subunits. c A cut-through view of the CMG-Pol epsilon reveals duplex DNA entering through the N-terminal domain of MCM and the leading-strand template captured within the ATPase domain. A 90° rotated view of the Mcm3-5-2 region reveals how C-Pol2/Dpb2 clamping stabilizes nucleotide binding and single-stranded DNA engagement by Mcm2, Mcm5 and Mcm3 pore loops

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