Extended Data Fig. 4: Comparison of starting predicted protein models with final structures after flexible fitting into density map. | Nature Microbiology

Extended Data Fig. 4: Comparison of starting predicted protein models with final structures after flexible fitting into density map.

From: In situ structure of a bacterial flagellar motor at subnanometre resolution reveals adaptations for increased torque

Extended Data Fig. 4

(a) AlphaFold2 (ref. 29) prediction of FlgP (dark grey) required bending of the oligomer to fit the curvature of the first ring of the basal disk (purple). (b) AlphaFold2 prediction of PflC1 required independent rigid-body docking of the N- and C-terminal domains (magenta). (c) The resulting N-terminal domain of PflC was rigid-body docked into density multiple times for PflC2–7. C-terminal domains were not modelled. Higher thresholds required for more peripheral, and presumably more flexible, components. (d) PflA and PflB AlphaFold2 models (dark grey) required bending to fit into density maps (pale and dark green for PflA and PflB, respectively).

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