Fig. 1: Structural information on rNadA.
A Deuterium uptake plots of representative peptides spanning distinct structural motifs of NadA and with distinct HDX rates (deuterium labeling times: 4 s, 15 s, 30 s, 1 min on ice and 1 min, 10 min, 30 min, 100 min, 1000 min at room temperature). Uptake values are normalized by the MaxD and expressed as % of deuteration. Source data are provided as a Source Data file. B Bimodal HDX kinetics of NadA. Isotopic distributions of peptides 40–59 (coiled coil, head) and 206–249 (coiled coil, stalk) upon deuterium labeling at room temperature. The dashed red line indicates the centroid mass of the maximally labeled state. C Proposed structural model of the stalk (aa 168–350). Black helices represent coiled coil heptad repeats, blue helices represent coiled coil undecad repeats, arrows indicate the flexible domains, and the black wavy line represents the disordered region of NadA tail. Residues colored in red are located in a position of heptad and undecad repeats, residues colored in green are located in d position in heptads, and residues colored in cyan are located in h position in undecads. D Different views of the cryo-EM map of rNadA (side views and top view) fitted with the crystal structure of NadA24-170 (PDB 6EUN).
