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. 2016 Apr 4;291(24):12467–12480. doi: 10.1074/jbc.M116.719591

FIGURE 1.

FIGURE 1.

Protein sequence coverage, experimental schematic, and HDX kinetic data. A, SsoMCM primary sequence, motifs, and domains. A, A-subdomain; B, B-subdomain; C, C-subdomain; ZBD, zinc-binding domain; N-C, N-terminal to C-terminal linker; WA, Walker A; WB, Walker B; S1, sensor 1; RF, arginine finger; S2, sensor 2; WH, winged helix. B, protease XIII digestion of apo-SsoMCM (576 peptides, 5–30 residues in length) was characterized, providing 98.7% sequence coverage. C, hexameric model and monomeric structure of SsoMCM (Protein Data Bank code 3F9V) highlighting the domains and motifs. D, schematic of the three experimental conditions for the HDX-MS experiments comparing MCM alone (SsoMCM Apo) (○), MCM and 3′-tail (□), or MCM and 3′-tail/5′-tail (♢) DNA substrates. E, ARDD (free minus bound) averaged over all HDX incubation periods. F, heat maps for SsoMCM under the three conditions showing the deuterium uptake level (as a percentage) calculated by ARDD.