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. 2018 Oct 15;37(22):e100005. doi: 10.15252/embj.2018100005

Figure EV3. The H5‐1/2 loop is flipped toward the C‐terminus of the ARM domain in Arp2/3‐bound SPIN90.

Figure EV3

  1. Cα trace of SPIN90 (351–722) superposed onto the structure of SPIN90 (269–722) from the co‐complex structure. His580 is shown in stick representation. H5‐1/2 is flipped away from the C‐terminus in the inactive 351–722 structure and toward it in the co‐complex structure.
  2. Zoomed in view from panel (A) showing the difference in conformation of the H5‐1/2 loop in the inactive (351–722, sticks with gray carbon atoms) versus active (269–722, sticks with cyan carbon atoms) SPIN90 structures. Positive (green) or negative (red) Fo−Fc electron density maps are contoured at ±2.0 σ and were generated from the co‐complex reflection file plus a PDB file in which H5‐1/2 loop (residues 577–585) of the co‐complex structure was replaced with the same residues from chain A in the 351–722 structure.