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. 2020 Jun 22;39(14):e104006. doi: 10.15252/embj.2019104006

Figure 1. Phalloidin‐bound F‐actin structure resembles ADP‐actin state.

Figure 1

  • A
    Surface representation of F‐actin–ADP model, five monomers marked as n series from barbed to pointed end. A phalloidin molecule (yellow stick representation) bound between three actin monomers is highlighted.
  • B
    Expanded view of phalloidin‐binding pocket as marked with red box in panel (A). The density of phalloidin from EM map is shown around the ligand.
  • C
    Comparison of phalloidin‐binding pocket residues between apo (in gray) and phalloidin bound (actin monomer colors as indicated in panel A) Key residues with their side chains and phalloidin are represented in stick representation.
  • D
    Overlay of F‐actin–ADP (gray), ADP/Phalloidin (blue), and ADP/Jasplakinolide (orange) shows the D‐loop conformations across different structures as indicated.